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2IWE

Structure of a cavity mutant (H117G) of Pseudomonas aeruginosa azurin

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0008270molecular_functionzinc ion binding
A0009055molecular_functionelectron transfer activity
A0042597cellular_componentperiplasmic space
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0046914molecular_functiontransition metal ion binding
D0005507molecular_functioncopper ion binding
D0005515molecular_functionprotein binding
D0005886cellular_componentplasma membrane
D0008270molecular_functionzinc ion binding
D0009055molecular_functionelectron transfer activity
D0042597cellular_componentperiplasmic space
D0042802molecular_functionidentical protein binding
D0046872molecular_functionmetal ion binding
D0046914molecular_functiontransition metal ion binding
G0005507molecular_functioncopper ion binding
G0005515molecular_functionprotein binding
G0005886cellular_componentplasma membrane
G0008270molecular_functionzinc ion binding
G0009055molecular_functionelectron transfer activity
G0042597cellular_componentperiplasmic space
G0042802molecular_functionidentical protein binding
G0046872molecular_functionmetal ion binding
G0046914molecular_functiontransition metal ion binding
J0005507molecular_functioncopper ion binding
J0005515molecular_functionprotein binding
J0005886cellular_componentplasma membrane
J0008270molecular_functionzinc ion binding
J0009055molecular_functionelectron transfer activity
J0042597cellular_componentperiplasmic space
J0042802molecular_functionidentical protein binding
J0046872molecular_functionmetal ion binding
J0046914molecular_functiontransition metal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 1129
ChainResidue
AGLY45
AHIS46
ACYS112
AMET121
A2IH1001

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN D 1129
ChainResidue
D2IH1001
DGLY45
DHIS46
DCYS112
DMET121

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN G 1129
ChainResidue
D2IH1001
GGLY45
GHIS46
GCYS112
GPHE114
GMET121

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN J 1129
ChainResidue
A2IH1001
JGLY45
JHIS46
JCYS112
JPHE114
JMET121

site_idAC5
Number of Residues19
DetailsBINDING SITE FOR RESIDUE 2IH A 1001
ChainResidue
AMET13
AVAL43
AMET44
AGLY45
AHIS46
ACYS112
APHE114
APRO115
AGLY116
AMET121
AZN1129
JVAL43
JMET44
JGLY45
JHIS46
JCYS112
JPHE114
JGLY116
JZN1129

site_idAC6
Number of Residues18
DetailsBINDING SITE FOR RESIDUE 2IH D 1001
ChainResidue
DVAL43
DMET44
DGLY45
DHIS46
DCYS112
DPHE114
DGLY116
DZN1129
GMET13
GVAL43
GMET44
GGLY45
GHIS46
GPHE114
GPRO115
GGLY116
GMET121
GZN1129

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues508
DetailsDomain: {"description":"Plastocyanin-like"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"1420141","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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