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2GI0

Crystal structure of Cu(I) Phe114Pro Azurin mutant

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
B0005507molecular_functioncopper ion binding
B0005515molecular_functionprotein binding
B0005886cellular_componentplasma membrane
B0008270molecular_functionzinc ion binding
B0009055molecular_functionelectron transfer activity
B0042597cellular_componentperiplasmic space
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
B0046914molecular_functiontransition metal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU1 A 200
ChainResidue
AHIS46
ACYS112
AHIS117
AMET121

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU1 B 200
ChainResidue
BHIS46
BCYS112
BHIS117
BMET121

Functional Information from PROSITE/UniProt
site_idPS00196
Number of Residues17
DetailsCOPPER_BLUE Type-1 copper (blue) proteins signature. GeqYmFFCtpPgHsal.M
ChainResidueDetails
AGLY105-MET121

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues254
DetailsDomain: {"description":"Plastocyanin-like"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"1420141","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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