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2NZA

Structure and Function Studies of Cytochrome P450 158A1 from Streptomyces coelicolor A3(2)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0020037molecular_functionheme binding
A0042440biological_processpigment metabolic process
A0046872molecular_functionmetal ion binding
B0004497molecular_functionmonooxygenase activity
B0005506molecular_functioniron ion binding
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0020037molecular_functionheme binding
B0042440biological_processpigment metabolic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE HEM A 430
ChainResidue
AARG74
ATYR321
AALA348
ATYR349
AGLY350
AHIS354
ACYS356
ATHR357
AALA362
AHOH470
AHOH501
ALEU96
AALA97
AHIS104
ALEU242
AGLY245
AGLY246
AALA248
AARG298

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE HEM B 430
ChainResidue
BARG74
BLEU96
BALA97
BHIS104
BPHE115
BGLY245
BALA248
BHIS290
BARG291
BARG298
BTYR321
BALA348
BGLY350
BHIS353
BHIS354
BPHE355
BCYS356
BALA362
BHOH465
BHOH505

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:17614370, ECO:0007744|PDB:2NZ5
ChainResidueDetails
AARG92
ATYR199
AHIS290
BARG92
BTYR199
BHIS290

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:17614370, ECO:0007744|PDB:2DKK, ECO:0007744|PDB:2NZ5, ECO:0007744|PDB:2NZA
ChainResidueDetails
ACYS356
BCYS356

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Involved in determining product regiospecificity => ECO:0000269|PubMed:22203090
ChainResidueDetails
ALYS90
BLYS90

222415

PDB entries from 2024-07-10

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