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1CP4

FORMATION, CRYSTAL STRUCTURE, AND REARRANGEMENT OF A CYTOCHROME P450-CAM IRON-PHENYL COMPLEX

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0006707biological_processcholesterol catabolic process
A0008395molecular_functionsteroid hydroxylase activity
A0016491molecular_functionoxidoreductase activity
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0018683molecular_functioncamphor 5-monooxygenase activity
A0019383biological_process(+)-camphor catabolic process
A0020037molecular_functionheme binding
A0036199molecular_functioncholest-4-en-3-one 26-monooxygenase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE HEM A 415
ChainResidue
APRO100
ATHR349
APHE350
AGLY351
ASER354
AHIS355
ALEU356
ACYS357
ABNZ416
AHOH511
AHOH652
ATHR101
AHOH707
AGLN108
AARG112
ALEU244
ATHR252
AVAL295
AASP297
AARG299

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BNZ A 416
ChainResidue
ALEU244
AGLY248
ATHR252
AHEM415
AHOH708

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGhGSHLCLG
ChainResidueDetails
APHE350-GLY359

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: axial binding residue
ChainResidueDetails
ALEU358

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 133
ChainResidueDetails
APRO187hydrogen bond donor, proton acceptor, proton donor, proton relay
ATHR252hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
AVAL253hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
ALEU358electrostatic stabiliser, hydrogen bond acceptor, metal ligand
AGLY359electrostatic stabiliser, hydrogen bond donor
AGLN360electrostatic stabiliser, hydrogen bond donor

218500

数据于2024-04-17公开中

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