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1XB8

Zn substituted form of D62C/K74C double mutant of Pseudomonas Aeruginosa Azurin

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
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
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 1001
ChainResidue
AGLY45
AHIS46
ACYS112
APHE114
AHIS117
AMET121

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN C 5001
ChainResidue
CPHE114
CHIS117
CMET121
CGLY45
CHIS46
CCYS112

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 Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:1420141
ChainResidueDetails
AHIS46
ACYS112
AHIS117
CHIS46
CCYS112
CHIS117

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AMET121
CMET121

219869

PDB entries from 2024-05-15

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