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4C9K

Structure of Camphor and Hydroxycamphor bound wild type CYP101D1

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0016020cellular_componentmembrane
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
B0016020cellular_componentmembrane
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 Residues18
DetailsBINDING SITE FOR RESIDUE HEM A 422
ChainResidue
APRO102
AASP305
AARG307
ATHR357
APRO362
AHIS363
ACYS365
AGLY367
ACAH423
AHOH2105
ATHR103
AHIS110
AARG114
APHE165
ALEU253
AGLY256
ATHR260
APHE264

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CAH A 423
ChainResidue
ATRP89
ATYR98
ALEU252
ALEU255
AGLY256
AVAL303
AHEM422

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CAH A 423
ChainResidue
ATRP89
ATYR98
ALEU252
ALEU255
AGLY256
AVAL303
AHEM422

site_idAC4
Number of Residues19
DetailsBINDING SITE FOR RESIDUE HEM B 422
ChainResidue
BPRO102
BTHR103
BHIS110
BARG114
BPHE165
BLEU253
BGLY256
BTHR260
BPHE297
BASP305
BARG307
BTHR357
BALA359
BPRO362
BHIS363
BCYS365
BGLY367
BCAH423
BHOH2077

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CAH B 423
ChainResidue
BTRP89
BTYR98
BLEU255
BGLY256
BHEM422

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CAH B 423
ChainResidue
BTRP89
BTYR98
BLEU255
BGLY256
BHEM422

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PDB entries from 2024-06-26

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