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1LYQ

Crystal Structure of PcoC, a Methionine Rich Copper Resistance Protein from Escherichia coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0006825biological_processcopper ion transport
A0042597cellular_componentperiplasmic space
A0046688biological_processresponse to copper ion
B0005507molecular_functioncopper ion binding
B0006825biological_processcopper ion transport
B0042597cellular_componentperiplasmic space
B0046688biological_processresponse to copper ion
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL A 1001
ChainResidue
AVAL32
BHOH1033
BHOH1034
ASER35
AVAL59
AHOH1017
AHOH1032
AHOH1063
AHOH1108
BVAL59
BHOH1021

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 1002
ChainResidue
ALEU5
AHOH1014
AHOH1022
AHOH1028
AHOH1039
AHOH1072
AHOH1099
AHOH1147

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 1004
ChainResidue
BASP13
BHOH1049
BHOH1142
BHOH1154

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 1005
ChainResidue
AMET44
ALYS45
AHOH1077
AHOH1109
AHOH1150
AHOH1152
BARG82
BHOH1079

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 1006
ChainResidue
ALYS6
ASER27
AGLU28
ALYS66

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17477524","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18421485","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P12376","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

238582

PDB entries from 2025-07-09

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