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2I7S

Crystal structure of Re(phen)(CO)3 (Thr124His)(His83Gln) Azurin Cu(II) from Pseudomonas aeruginosa

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
C0005507molecular_functioncopper ion binding
C0005515molecular_functionprotein binding
C0008270molecular_functionzinc ion binding
C0009055molecular_functionelectron transfer activity
C0042597cellular_componentperiplasmic space
C0042802molecular_functionidentical protein binding
C0046872molecular_functionmetal ion binding
C0046914molecular_functiontransition metal ion binding
D0005507molecular_functioncopper ion binding
D0005515molecular_functionprotein binding
D0008270molecular_functionzinc ion binding
D0009055molecular_functionelectron transfer activity
D0042597cellular_componentperiplasmic space
D0042802molecular_functionidentical protein binding
D0046872molecular_functionmetal ion binding
D0046914molecular_functiontransition metal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU A 901
ChainResidue
AGLY45
AHIS46
ACYS112
AHIS117
AMET121

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU B 902
ChainResidue
BMET321
BGLY245
BHIS246
BCYS312
BHIS317

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU C 903
ChainResidue
CGLY445
CHIS446
CCYS512
CHIS517
CMET521

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU D 904
ChainResidue
DGLY645
DHIS646
DCYS712
DHIS717
DMET721

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE REP A 801
ChainResidue
AMET109
AHIS124
AHOH1413
BGLN307
BREP802

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE REP B 802
ChainResidue
AGLN107
AHIS124
AREP801
BMET309
BHIS324
BHOH1164
BHOH1239
BHOH1378

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE REP C 803
ChainResidue
CMET509
CLYS522
CHIS524
CHOH1188
CHOH1223
DGLN707
DHIS724
DREP804

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE REP D 804
ChainResidue
CGLN507
CHIS524
CREP803
DMET709
DHIS724

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CON B 850
ChainResidue
BASP276
BASP277
BVAL280
BILE281
BHOH1301
BHOH1361

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:1420141
ChainResidueDetails
AHIS46
DHIS646
DCYS712
DHIS717
ACYS112
AHIS117
BHIS246
BCYS312
BHIS317
CHIS446
CCYS512
CHIS517

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING:
ChainResidueDetails
AMET121
BMET321
CMET521
DMET721

222036

PDB entries from 2024-07-03

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