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6WE6

Camphor bound P450cam D251E structure

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
B0004497molecular_functionmonooxygenase activity
B0005506molecular_functioniron ion binding
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0006707biological_processcholesterol catabolic process
B0008395molecular_functionsteroid hydroxylase activity
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0018683molecular_functioncamphor 5-monooxygenase activity
B0019383biological_process(+)-camphor catabolic process
B0020037molecular_functionheme binding
B0036199molecular_functioncholest-4-en-3-one 26-monooxygenase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue HEM A 501
ChainResidue
ATHR101
ATHR349
APHE350
AGLY351
AHIS355
ACYS357
ACAM502
AHOH672
AGLN108
AARG112
ALEU244
ALEU245
ATHR252
AASP297
AARG299
AGLN322

site_idAC2
Number of Residues4
Detailsbinding site for residue CAM A 502
ChainResidue
APHE87
ATYR96
AVAL247
AHEM501

site_idAC3
Number of Residues6
Detailsbinding site for residue K A 503
ChainResidue
AGLU84
AGLY93
AGLU94
ATYR96
AHOH763
AHOH767

site_idAC4
Number of Residues18
Detailsbinding site for residue HEM B 501
ChainResidue
BTHR101
BGLN108
BARG112
BLEU245
BGLY248
BGLY249
BTHR252
BVAL295
BASP297
BARG299
BGLN322
BTHR349
BPHE350
BGLY351
BHIS355
BCYS357
BCAM502
BHOH653

site_idAC5
Number of Residues4
Detailsbinding site for residue CAM B 502
ChainResidue
BPHE87
BTYR96
BLEU244
BHEM501

site_idAC6
Number of Residues5
Detailsbinding site for residue K B 503
ChainResidue
BGLU84
BGLY93
BGLU94
BTYR96
BHOH692

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
BCYS357
ACYS357

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 133
ChainResidueDetails
AARG186hydrogen bond donor, proton acceptor, proton donor, proton relay
AGLU251hydrogen 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
BARG186hydrogen bond donor, proton acceptor, proton donor, proton relay
BGLU251hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
BTHR252hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
BCYS357electrostatic stabiliser, hydrogen bond acceptor, metal ligand
BLEU358electrostatic stabiliser, hydrogen bond donor
BGLY359electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2024-05-15

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