Zinc in PDB 2xoz: C-Terminal Cysteine Rich Domain of Human Chfr Bound to Amp

The structure of C-Terminal Cysteine Rich Domain of Human Chfr Bound to Amp, PDB code: 2xoz was solved by J.Oberoi, R.Bayliss, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.687 / 2.37
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	162.810, 51.560, 82.490, 90.00, 105.93, 90.00
R / Rfree (%)	17.93 / 23.15

The binding sites of Zinc atom in the C-Terminal Cysteine Rich Domain of Human Chfr Bound to Amp (pdb code 2xoz). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 10 binding sites of Zinc where determined in the C-Terminal Cysteine Rich Domain of Human Chfr Bound to Amp, PDB code: 2xoz:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Zinc binding site 1 out of 10 in the C-Terminal Cysteine Rich Domain of Human Chfr Bound to Amp


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of C-Terminal Cysteine Rich Domain of Human Chfr Bound to Amp within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn991 b:31.2 occ:1.00 NE2 A:HIS482 2.1 20.2 1.0 SG A:CYS428 2.4 27.0 1.0 SG A:CYS476 2.4 31.8 1.0 SG A:CYS431 2.5 36.9 1.0 CD2 A:HIS482 2.8 20.0 1.0 CE1 A:HIS482 3.2 34.0 1.0 CB A:CYS428 3.3 30.6 1.0 CB A:CYS431 3.4 36.7 1.0 CB A:CYS476 3.5 39.7 1.0 N A:CYS431 3.6 40.3 1.0 CA A:CYS431 3.7 41.3 1.0 N A:CYS428 3.8 29.7 1.0 O A:HOH2006 3.8 29.8 1.0 CA A:CYS428 4.0 27.4 1.0 CG A:HIS482 4.1 27.8 1.0 C A:GLN430 4.1 37.7 1.0 ND1 A:HIS482 4.2 33.7 1.0 O A:CYS428 4.4 30.0 1.0 C A:CYS428 4.5 24.3 1.0 O A:GLN430 4.6 31.3 1.0 N A:GLN430 4.7 33.2 1.0 CA A:GLN430 4.8 37.2 1.0 C A:VAL427 4.9 33.4 1.0 CA A:CYS476 4.9 40.1 1.0 N A:PRO493 5.0 23.7 1.0

Zinc binding site 2 out of 10 in the C-Terminal Cysteine Rich Domain of Human Chfr Bound to Amp


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of C-Terminal Cysteine Rich Domain of Human Chfr Bound to Amp within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn992 b:19.9 occ:1.00 SG A:CYS518 2.3 18.4 1.0 SG A:CYS488 2.4 22.7 1.0 SG A:CYS485 2.5 16.3 1.0 SG A:CYS524 2.5 17.3 1.0 CB A:CYS524 3.1 13.4 1.0 CB A:CYS485 3.2 18.0 1.0 CB A:CYS488 3.4 20.8 1.0 CB A:CYS518 3.5 21.2 1.0 O A:HOH2026 3.8 17.8 1.0 N A:CYS488 3.8 20.3 1.0 N A:CYS518 4.0 13.3 1.0 CA A:CYS524 4.0 20.9 1.0 ZN A:ZN993 4.1 20.3 1.0 CA A:CYS518 4.2 19.2 1.0 CA A:CYS488 4.2 24.9 1.0 CB A:CYS487 4.5 17.3 1.0 SG A:CYS532 4.6 19.6 1.0 C A:CYS518 4.7 18.0 1.0 CA A:CYS485 4.7 17.5 1.0 N A:HIS519 4.7 14.6 1.0 C A:CYS487 4.9 23.9 1.0 N A:THR525 4.9 26.4 1.0 C A:CYS524 5.0 22.1 1.0

Zinc binding site 3 out of 10 in the C-Terminal Cysteine Rich Domain of Human Chfr Bound to Amp


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of C-Terminal Cysteine Rich Domain of Human Chfr Bound to Amp within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn993 b:20.3 occ:1.00 SG A:CYS487 2.3 21.9 1.0 SG A:CYS524 2.4 17.3 1.0 SG A:CYS532 2.4 19.6 1.0 SG A:CYS529 2.4 21.1 1.0 CB A:CYS487 3.0 17.3 1.0 CB A:CYS532 3.1 16.4 1.0 CB A:CYS524 3.3 13.4 1.0 CB A:CYS529 3.3 17.2 1.0 ZN A:ZN992 4.1 19.9 1.0 N A:CYS532 4.2 14.9 1.0 CA A:CYS532 4.3 16.0 1.0 CA A:CYS487 4.4 21.1 1.0 N A:CYS488 4.6 20.3 1.0 CA A:CYS529 4.7 22.2 1.0 CA A:CYS524 4.7 20.9 1.0 C A:CYS487 4.7 23.9 1.0 SG A:CYS485 4.8 16.3 1.0 C A:CYS524 4.8 22.1 1.0 CB A:CYS488 5.0 20.8 1.0

Zinc binding site 4 out of 10 in the C-Terminal Cysteine Rich Domain of Human Chfr Bound to Amp


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of C-Terminal Cysteine Rich Domain of Human Chfr Bound to Amp within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn994 b:20.3 occ:1.00 SG A:CYS604 2.3 18.8 1.0 SG A:CYS513 2.3 17.3 1.0 SG A:CYS601 2.3 20.0 1.0 SG A:CYS510 2.3 15.2 1.0 CB A:CYS510 3.0 20.4 1.0 CB A:CYS513 3.2 22.2 1.0 CB A:CYS604 3.3 11.5 1.0 CB A:CYS601 3.5 10.6 1.0 N A:CYS513 3.7 20.3 1.0 N A:CYS601 3.9 15.7 1.0 CA A:CYS513 4.0 23.9 1.0 N A:CYS604 4.1 13.7 1.0 O A:HOH2066 4.1 28.5 1.0 CA A:CYS601 4.3 18.6 1.0 CA A:CYS604 4.3 12.0 1.0 CA A:CYS510 4.5 20.1 1.0 CB A:VAL512 4.6 24.3 1.0 CE2 A:PHE517 4.7 18.7 1.0 C A:VAL512 4.8 20.5 1.0 C A:CYS513 4.9 18.8 1.0 CZ A:PHE517 4.9 14.1 1.0 C A:CYS601 5.0 19.0 1.0

Zinc binding site 5 out of 10 in the C-Terminal Cysteine Rich Domain of Human Chfr Bound to Amp


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of C-Terminal Cysteine Rich Domain of Human Chfr Bound to Amp within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn995 b:12.8 occ:1.00 NE2 A:HIS655 2.0 13.8 1.0 NE2 A:HIS649 2.0 10.9 1.0 SG A:CYS635 2.3 11.0 1.0 SG A:CYS641 2.4 13.4 1.0 CD2 A:HIS649 2.9 14.5 1.0 CE1 A:HIS655 3.0 8.7 1.0 CD2 A:HIS655 3.0 13.7 1.0 CE1 A:HIS649 3.0 11.6 1.0 CB A:CYS641 3.2 12.5 1.0 CB A:CYS635 3.2 14.5 1.0 ND1 A:HIS655 4.1 12.3 1.0 CG A:HIS649 4.1 11.9 1.0 ND1 A:HIS649 4.1 15.8 1.0 CG A:HIS655 4.1 13.1 1.0 CA A:CYS635 4.6 18.7 1.0 CA A:CYS641 4.6 13.5 1.0 CB A:GLN644 4.7 10.0 1.0 N A:GLN644 4.7 17.9 1.0 CD1 A:TRP637 4.8 12.2 1.0 CB A:THR643 4.8 12.0 1.0 CB A:TRP637 5.0 9.2 1.0

Zinc binding site 6 out of 10 in the C-Terminal Cysteine Rich Domain of Human Chfr Bound to Amp


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of C-Terminal Cysteine Rich Domain of Human Chfr Bound to Amp within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn991 b:17.3 occ:1.00 NE2 B:HIS482 2.1 18.0 1.0 SG B:CYS476 2.3 20.5 1.0 SG B:CYS428 2.4 13.7 1.0 SG B:CYS431 2.5 19.8 1.0 CD2 B:HIS482 2.9 16.1 1.0 CE1 B:HIS482 3.2 22.1 1.0 CB B:CYS476 3.3 24.3 1.0 CB B:CYS428 3.5 12.1 1.0 N B:CYS431 3.5 16.3 1.0 CB B:CYS431 3.6 20.0 1.0 CA B:CYS431 3.7 17.6 1.0 N B:CYS428 3.8 14.2 1.0 CA B:CYS428 4.1 16.4 1.0 O B:HOH2006 4.1 21.9 1.0 C B:GLN430 4.2 18.7 1.0 CG B:HIS482 4.2 21.9 1.0 ND1 B:HIS482 4.3 24.3 1.0 O B:CYS428 4.4 18.0 1.0 C B:CYS428 4.5 19.7 1.0 N B:GLN430 4.7 15.8 1.0 CA B:CYS476 4.7 25.4 1.0 O B:GLN430 4.7 23.8 1.0 CA B:GLN430 4.8 19.4 1.0 CB B:GLN430 4.9 18.1 1.0 C B:VAL427 4.9 24.4 1.0 N B:PRO493 4.9 13.1 1.0 CB B:PRO493 4.9 16.1 1.0 CD B:PRO493 4.9 15.7 1.0 CA B:PRO493 5.0 14.2 1.0

Zinc binding site 7 out of 10 in the C-Terminal Cysteine Rich Domain of Human Chfr Bound to Amp


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 7 of C-Terminal Cysteine Rich Domain of Human Chfr Bound to Amp within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn992 b:15.6 occ:1.00 SG B:CYS485 2.3 18.7 1.0 SG B:CYS518 2.3 13.0 1.0 SG B:CYS488 2.4 18.7 1.0 SG B:CYS524 2.4 17.4 1.0 CB B:CYS485 3.1 12.5 1.0 CB B:CYS524 3.2 17.3 1.0 CB B:CYS488 3.3 17.4 1.0 CB B:CYS518 3.4 12.4 1.0 N B:CYS488 3.8 17.6 1.0 N B:CYS518 3.9 13.9 1.0 O B:HOH2029 4.0 23.8 1.0 ZN B:ZN993 4.0 17.4 1.0 CA B:CYS524 4.0 17.4 1.0 CA B:CYS488 4.1 14.8 1.0 O B:HOH2009 4.1 18.2 1.0 CA B:CYS518 4.2 17.5 1.0 SG B:CYS532 4.4 15.2 1.0 CA B:CYS485 4.5 14.5 1.0 N B:HIS519 4.7 15.6 1.0 C B:CYS518 4.7 17.4 1.0 CB B:CYS487 4.7 16.9 1.0 C B:CYS487 4.8 22.1 1.0 SG B:CYS487 4.9 20.0 1.0 C B:CYS488 5.0 19.3 1.0

Zinc binding site 8 out of 10 in the C-Terminal Cysteine Rich Domain of Human Chfr Bound to Amp


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 8 of C-Terminal Cysteine Rich Domain of Human Chfr Bound to Amp within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn993 b:17.4 occ:1.00 SG B:CYS487 2.3 20.0 1.0 SG B:CYS529 2.3 19.5 1.0 SG B:CYS532 2.3 15.2 1.0 SG B:CYS524 2.4 17.4 1.0 CB B:CYS487 3.1 16.9 1.0 CB B:CYS532 3.1 12.9 1.0 CB B:CYS524 3.2 17.3 1.0 CB B:CYS529 3.2 20.3 1.0 N B:CYS532 4.0 14.3 1.0 ZN B:ZN992 4.0 15.6 1.0 CA B:CYS532 4.2 16.3 1.0 CA B:CYS487 4.5 17.8 1.0 CA B:CYS529 4.5 23.9 1.0 N B:CYS488 4.6 17.6 1.0 CA B:CYS524 4.6 17.4 1.0 SG B:CYS485 4.6 18.7 1.0 C B:CYS487 4.7 22.1 1.0 C B:CYS524 4.9 21.4 1.0 CB B:CYS488 5.0 17.4 1.0

Zinc binding site 9 out of 10 in the C-Terminal Cysteine Rich Domain of Human Chfr Bound to Amp


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 9 of C-Terminal Cysteine Rich Domain of Human Chfr Bound to Amp within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn994 b:16.8 occ:1.00 SG B:CYS510 2.3 10.4 1.0 SG B:CYS604 2.4 18.1 1.0 SG B:CYS601 2.4 13.2 1.0 SG B:CYS513 2.4 18.4 1.0 CB B:CYS510 3.1 16.2 1.0 CB B:CYS604 3.2 12.6 1.0 CB B:CYS513 3.4 9.4 1.0 CB B:CYS601 3.5 14.4 1.0 N B:CYS513 3.7 12.0 1.0 N B:CYS601 4.0 13.0 1.0 CA B:CYS513 4.1 13.9 1.0 N B:CYS604 4.3 12.5 1.0 CA B:CYS601 4.4 12.7 1.0 CA B:CYS604 4.4 12.7 1.0 O B:HOH2022 4.4 29.0 1.0 CA B:CYS510 4.6 15.0 1.0 CB B:VAL512 4.6 11.4 1.0 C B:VAL512 4.8 14.1 1.0 OE1 B:GLN515 4.9 22.3 0.6 C B:CYS513 4.9 14.2 1.0 N B:LEU514 5.0 14.9 1.0 C B:CYS601 5.0 16.7 1.0

Zinc binding site 10 out of 10 in the C-Terminal Cysteine Rich Domain of Human Chfr Bound to Amp


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 10 of C-Terminal Cysteine Rich Domain of Human Chfr Bound to Amp within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn995 b:12.2 occ:1.00 NE2 B:HIS649 2.0 13.8 1.0 NE2 B:HIS655 2.1 10.3 1.0 SG B:CYS635 2.2 18.1 1.0 SG B:CYS641 2.4 10.7 1.0 CE1 B:HIS649 3.0 19.3 1.0 CD2 B:HIS649 3.1 15.1 1.0 CD2 B:HIS655 3.1 10.1 1.0 CE1 B:HIS655 3.1 11.7 1.0 CB B:CYS641 3.2 14.2 1.0 CB B:CYS635 3.2 13.8 1.0 ND1 B:HIS649 4.1 21.9 1.0 CG B:HIS649 4.2 15.2 1.0 ND1 B:HIS655 4.2 13.6 1.0 CG B:HIS655 4.3 10.4 1.0 CD1 B:TRP637 4.3 38.0 1.0 CA B:CYS635 4.6 18.5 1.0 CA B:CYS641 4.6 19.4 1.0 N B:GLN644 4.6 20.4 1.0 CB B:GLN644 4.7 11.9 1.0 CB B:THR643 4.8 18.7 1.0 CA B:GLN644 4.9 15.1 1.0 CB B:TRP637 4.9 21.2 1.0 N6 B:AMP1664 4.9 26.7 1.0 N1 B:AMP1665 4.9 34.5 1.0 CB B:PHE653 5.0 13.9 1.0

J.Oberoi, M.W.Richards, S.Crumpler, N.Brown, J.Blagg, R.Bayliss. Structural Basis of Poly(Adp-Ribose) Recognition By the Multizinc Binding Domain of Checkpoint with Forkhead-Associated and Ring Domains (Chfr). J.Biol.Chem. V. 285 39348 2010.
ISSN: ISSN 0021-9258
PubMed: 20880844
DOI: 10.1074/JBC.M110.159855