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Zinc in PDB 2md8: uc(Nmr) Structure of SP140 Phd Finger Cis Conformer

Zinc Binding Sites:

The binding sites of Zinc atom in the uc(Nmr) Structure of SP140 Phd Finger Cis Conformer (pdb code 2md8). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the uc(Nmr) Structure of SP140 Phd Finger Cis Conformer, PDB code: 2md8:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2md8

Go back to Zinc Binding Sites List in 2md8
Zinc binding site 1 out of 2 in the uc(Nmr) Structure of SP140 Phd Finger Cis Conformer


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of uc(Nmr) Structure of SP140 Phd Finger Cis Conformer within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn101

b:0.2
occ:1.00
SG C:CYS48 2.3 0.2 1.0
SG C:CYS51 2.3 0.3 1.0
SG C:CYS23 2.3 0.2 1.0
SG C:CYS26 2.3 0.2 1.0
H C:CYS23 2.8 0.2 1.0
HB2 C:CYS23 3.2 0.2 1.0
HB2 C:CYS51 3.2 0.2 1.0
HB3 C:CYS48 3.3 0.2 1.0
CB C:CYS48 3.3 0.2 1.0
HB2 C:CYS26 3.3 0.2 1.0
CB C:CYS23 3.4 0.2 1.0
CB C:CYS51 3.4 0.2 1.0
CB C:CYS26 3.4 0.2 1.0
HB2 C:CYS48 3.4 0.3 1.0
H C:CYS51 3.5 0.2 1.0
N C:CYS23 3.7 0.2 1.0
HB3 C:CYS26 3.7 0.2 1.0
N C:CYS51 4.1 0.3 1.0
HA C:CYS22 4.1 0.3 1.0
CA C:CYS23 4.1 0.2 1.0
HB3 C:CYS51 4.2 0.3 1.0
HB3 C:CYS23 4.2 0.3 1.0
HB2 C:PHE50 4.2 0.4 1.0
CA C:CYS51 4.3 0.3 1.0
H C:CYS26 4.4 0.1 1.0
HA C:CYS51 4.5 0.4 1.0
CA C:CYS48 4.7 0.3 1.0
C C:CYS22 4.7 0.2 1.0
CA C:CYS26 4.8 0.2 1.0
OG C:SER56 4.8 8.3 1.0
CA C:CYS22 4.9 0.2 1.0
HA C:CYS23 4.9 0.2 1.0
HB3 C:PHE50 4.9 0.5 1.0
HB3 C:CYS22 4.9 0.8 1.0
N C:CYS26 5.0 0.2 1.0

Zinc binding site 2 out of 2 in 2md8

Go back to Zinc Binding Sites List in 2md8
Zinc binding site 2 out of 2 in the uc(Nmr) Structure of SP140 Phd Finger Cis Conformer


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of uc(Nmr) Structure of SP140 Phd Finger Cis Conformer within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn102

b:0.3
occ:1.00
NE2 C:HIS35 2.0 0.4 1.0
NE2 C:HIS31 2.0 0.4 1.0
SG C:CYS11 2.3 0.3 1.0
SG C:CYS14 2.3 0.4 1.0
CE1 C:HIS35 2.5 0.4 1.0
CE1 C:HIS31 2.6 0.4 1.0
HE1 C:HIS35 2.8 0.4 1.0
HE1 C:HIS31 2.8 0.5 1.0
CD2 C:HIS35 2.9 0.4 1.0
CD2 C:HIS31 2.9 0.3 1.0
HB2 C:CYS14 3.2 0.3 1.0
CB C:CYS11 3.3 0.4 1.0
HB3 C:CYS11 3.3 0.5 1.0
CB C:CYS14 3.4 0.3 1.0
HD2 C:HIS35 3.4 0.4 1.0
HB2 C:CYS11 3.4 0.5 1.0
HD2 C:HIS31 3.4 0.4 1.0
H C:CYS14 3.5 0.3 1.0
ND1 C:HIS35 3.5 0.4 1.0
ND1 C:HIS31 3.5 0.3 1.0
CG C:HIS35 3.7 0.4 1.0
HD11 C:LEU20 3.7 1.1 1.0
CG C:HIS31 3.7 0.3 1.0
N C:CYS14 4.1 0.2 1.0
HB C:VAL13 4.1 0.9 1.0
HB3 C:CYS14 4.2 0.4 1.0
CA C:CYS14 4.2 0.2 1.0
HG C:LEU20 4.3 0.7 1.0
HD1 C:HIS35 4.3 0.4 1.0
HD1 C:HIS31 4.3 0.4 1.0
HA C:CYS14 4.4 0.3 1.0
HD12 C:LEU20 4.5 1.2 1.0
CD1 C:LEU20 4.5 0.6 1.0
O C:HIS31 4.7 0.2 1.0
CA C:CYS11 4.7 0.4 1.0
CG C:LEU20 4.9 0.4 1.0
HB2 C:LEU20 5.0 0.5 1.0

Reference:

C.Zucchelli, S.Tamburri, G.Quilici, E.Palagano, A.Berardi, M.Saare, P.Peterson, A.Bachi, G.Musco. Structure of Human SP140 Phd Finger: An Atypical Fold Interacting with PIN1. Febs J. V. 281 216 2014.
ISSN: ISSN 1742-464X
PubMed: 24267382
DOI: 10.1111/FEBS.12588
Page generated: Wed Dec 16 03:40:03 2020

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