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3WRH

Crystal structure of P450cam

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
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
E0004497molecular_functionmonooxygenase activity
E0005506molecular_functioniron ion binding
E0005515molecular_functionprotein binding
E0005737cellular_componentcytoplasm
E0006707biological_processcholesterol catabolic process
E0008395molecular_functionsteroid hydroxylase activity
E0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
E0018683molecular_functioncamphor 5-monooxygenase activity
E0019383biological_process(+)-camphor catabolic process
E0020037molecular_functionheme binding
E0036199molecular_functioncholest-4-en-3-one 26-monooxygenase activity
E0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEM A 501
ChainResidue
APRO100
ATHR349
APHE350
AGLY351
AHIS355
ACYS357
AGLY359
ACAM503
AHOH610
AHOH804
ATHR101
AGLN108
AARG112
AGLY248
ATHR252
AASP297
AARG299
AGLN322

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K A 502
ChainResidue
AGLU84
AGLY93
AGLU94
ATYR96
AHOH695

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CAM A 503
ChainResidue
APHE87
ATYR96
ALEU244
AVAL247
AHEM501

site_idAC4
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HEM E 501
ChainResidue
EPRO100
ETHR101
EGLN108
EARG112
EGLY248
ETHR252
EASP297
EARG299
EGLN322
ETHR349
EPHE350
EGLY351
EHIS355
ECYS357
EGLY359
ECAM503
EHOH613

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K E 502
ChainResidue
EGLU84
EGLY93
EGLU94
ETYR96

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CAM E 503
ChainResidue
EPHE87
ETYR96
ELEU244
EVAL295
EHEM501

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 Residues2
DetailsBINDING: axial binding residue
ChainResidueDetails
ACYS357
ECYS357

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 133
ChainResidueDetails
AARG186hydrogen bond donor, proton acceptor, proton donor, proton relay
AASP251hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
ATHR252hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
ACYS357electrostatic stabiliser, hydrogen bond acceptor, metal ligand
ALEU358electrostatic stabiliser, hydrogen bond donor
AGLY359electrostatic stabiliser, hydrogen bond donor

site_idMCSA2
Number of Residues6
DetailsM-CSA 133
ChainResidueDetails
EARG186hydrogen bond donor, proton acceptor, proton donor, proton relay
EASP251hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
ETHR252hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
ECYS357electrostatic stabiliser, hydrogen bond acceptor, metal ligand
ELEU358electrostatic stabiliser, hydrogen bond donor
EGLY359electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2024-06-12

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