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2HX7

Crystal structure of Cu(II) Azurin with the metal-binding loop sequence "CTFPGHSALM" replaced with "CSPHQGAGM"

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0005515molecular_functionprotein binding
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
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 Residues5
DetailsBINDING SITE FOR RESIDUE CU A 201
ChainResidue
AGLY45
AHIS46
ACYS112
AHIS115
AMET120

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU B 201
ChainResidue
BMET120
BGLY45
BHIS46
BCYS112
BHIS115

Functional Information from PROSITE/UniProt
site_idPS00196
Number of Residues16
DetailsCOPPER_BLUE Type-1 copper (blue) proteins signature. GeqYmFFCs.P.HqgagM
ChainResidueDetails
AGLY105-MET120

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:1420141
ChainResidueDetails
AHIS46
ACYS112
AGLY117
BHIS46
BCYS112
BGLY117

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING:
ChainResidueDetails
ALYS121
BLYS121

226707

PDB entries from 2024-10-30

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