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1A4B

AZURIN MUTANT WITH MET 121 REPLACED BY HIS, PH 6.5 CRYSTAL FORM, DATA COLLECTED AT-180 DEGREES CELSIUS

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0009055molecular_functionelectron transfer activity
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
B0005507molecular_functioncopper ion binding
B0009055molecular_functionelectron transfer activity
B0042597cellular_componentperiplasmic space
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU A 130
ChainResidue
AHIS46
ACYS112
AHIS117
AHIS121

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 131
ChainResidue
AHOH295
AHOH302
AALA75
AGLY76
AHIS83
AHOH161
AHOH171

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU B 130
ChainResidue
BHIS46
BCYS112
BHIS117
BHIS121

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 131
ChainResidue
BALA75
BGLY76
BHIS83
BHOH154
BHOH219
BHOH267
BHOH275

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:3210236
ChainResidueDetails
AHIS46
ACYS112
BHIS46
AHIS117
AHIS121
BCYS112
BHIS117
BHIS121

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PDB entries from 2024-04-17

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