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Zinc in PDB 9jr9: Electronic Microscopy Structure of Human SCHLAFEN14-E211A Dimer

Zinc Binding Sites:

The binding sites of Zinc atom in the Electronic Microscopy Structure of Human SCHLAFEN14-E211A Dimer (pdb code 9jr9). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Electronic Microscopy Structure of Human SCHLAFEN14-E211A Dimer, PDB code: 9jr9:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 9jr9

Go back to Zinc Binding Sites List in 9jr9
Zinc binding site 1 out of 2 in the Electronic Microscopy Structure of Human SCHLAFEN14-E211A Dimer


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Electronic Microscopy Structure of Human SCHLAFEN14-E211A Dimer within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1001

b:60.2
occ:1.00
ND1 A:HIS282 2.1 46.5 1.0
SG A:CYS318 2.3 47.4 1.0
SG A:CYS284 2.3 53.8 1.0
SG A:CYS319 2.3 47.5 1.0
CE1 A:HIS282 2.6 46.5 1.0
CG A:HIS282 3.3 46.5 1.0
CB A:CYS318 3.4 47.4 1.0
CB A:CYS319 3.5 47.5 1.0
CB A:CYS284 3.8 53.8 1.0
NE2 A:HIS282 3.9 46.5 1.0
N A:CYS319 3.9 47.5 1.0
CB A:HIS282 4.0 46.5 1.0
N A:CYS284 4.1 53.8 1.0
CD A:PRO288 4.1 48.1 1.0
C A:CYS318 4.1 47.4 1.0
CD2 A:HIS282 4.2 46.5 1.0
CA A:HIS282 4.3 46.5 1.0
N A:PHE283 4.3 49.2 1.0
CA A:CYS319 4.3 47.5 1.0
CA A:CYS318 4.3 47.4 1.0
CE2 A:PHE317 4.5 43.7 1.0
CA A:CYS284 4.5 53.8 1.0
CG A:PRO288 4.7 48.1 1.0
O A:CYS318 4.7 47.4 1.0
C A:HIS282 4.7 46.5 1.0
CA A:LYS287 4.8 51.4 1.0
N A:CYS318 4.9 47.4 1.0
N A:LYS287 5.0 51.4 1.0

Zinc binding site 2 out of 2 in 9jr9

Go back to Zinc Binding Sites List in 9jr9
Zinc binding site 2 out of 2 in the Electronic Microscopy Structure of Human SCHLAFEN14-E211A Dimer


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Electronic Microscopy Structure of Human SCHLAFEN14-E211A Dimer within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1001

b:62.7
occ:1.00
ND1 B:HIS282 2.1 48.7 1.0
SG B:CYS318 2.3 48.4 1.0
SG B:CYS284 2.3 55.3 1.0
SG B:CYS319 2.3 48.9 1.0
CE1 B:HIS282 2.7 48.7 1.0
CG B:HIS282 3.3 48.7 1.0
CB B:CYS319 3.3 48.9 1.0
CB B:CYS318 3.6 48.4 1.0
N B:CYS319 3.8 48.9 1.0
CB B:CYS284 3.8 55.3 1.0
NE2 B:HIS282 3.9 48.7 1.0
CB B:HIS282 4.0 48.7 1.0
CD B:PRO288 4.2 50.3 1.0
CA B:CYS319 4.2 48.9 1.0
CA B:HIS282 4.2 48.7 1.0
N B:CYS284 4.2 55.3 1.0
CD2 B:HIS282 4.2 48.7 1.0
N B:PHE283 4.3 51.0 1.0
C B:CYS318 4.3 48.4 1.0
CA B:CYS318 4.5 48.4 1.0
CG B:PRO288 4.6 50.3 1.0
CA B:CYS284 4.6 55.3 1.0
CZ B:PHE317 4.7 45.4 1.0
C B:HIS282 4.7 48.7 1.0
CE1 B:PHE317 4.8 45.4 1.0

Reference:

M.Li, D.Sun, W.Hao, H.Fu, Y.Zhang, Z.Li, B.Qin, Y.Wang, S.Cui. Human Schlafen 14 Cleavage of Short Double-Stranded Rnas Underpins Its Antiviral Activity. Adv Sci 01727 2025.
ISSN: ESSN 2198-3844
PubMed: 40642785
DOI: 10.1002/ADVS.202501727
Page generated: Fri Aug 22 18:25:27 2025

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