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2VE4

Substrate free cyanobacterial CYP120A1

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0016125biological_processsterol metabolic process
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
B0004497molecular_functionmonooxygenase activity
B0005506molecular_functioniron ion binding
B0016125biological_processsterol metabolic process
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0020037molecular_functionheme binding
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE HEM A 1442
ChainResidue
ALEU93
ATYR344
AILE346
APRO383
APHE384
AGLY385
AARG389
ACYS391
AGLY393
APHE396
AALA397
AHIS101
AHOH2075
AARG105
AALA254
AGLY255
ATHR258
ALEU259
AVAL318
AARG323

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE HEM B 1443
ChainResidue
BLEU93
BHIS101
BARG105
BPHE159
BLEU251
BALA254
BGLY255
BTHR258
BPRO317
BVAL318
BARG323
BTYR344
BPRO383
BPHE384
BGLY385
BARG389
BCYS391
BGLY393
BPHE396
BHOH2084

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGgGLRECLG
ChainResidueDetails
APHE384-GLY393

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000250
ChainResidueDetails
ACYS391
BCYS391

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1akd
ChainResidueDetails
AGLU257
ATHR258

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1akd
ChainResidueDetails
BGLU257
BTHR258

222036

PDB entries from 2024-07-03

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