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4C9L

Structure of Cyanide and Camphor 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 Residues21
DetailsBINDING SITE FOR RESIDUE HEM A 1418
ChainResidue
APRO102
AVAL261
APHE264
AASP305
AARG307
ATHR357
AALA359
APRO362
AHIS363
ACYS365
AGLY367
ATHR103
ACYN1420
AHOH2183
AHIS110
AARG114
APHE165
ALEU253
AGLY256
AGLY257
ATHR260

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CAM A 1419
ChainResidue
ATRP89
ATYR98
ATHR187
ALEU255
AVAL303
ACYN1420

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CYN A 1420
ChainResidue
AGLY256
ATHR260
AHEM1418
ACAM1419
AHOH2388

site_idAC4
Number of Residues20
DetailsBINDING SITE FOR RESIDUE HEM B 1418
ChainResidue
BPRO102
BTHR103
BHIS110
BARG114
BPHE165
BLEU253
BGLY256
BGLY257
BTHR260
BVAL261
BPHE264
BPHE297
BASP305
BARG307
BTHR357
BHIS363
BCYS365
BGLY367
BCYN1420
BHOH2159

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CAM B 1419
ChainResidue
BTRP89
BTYR98
BTHR187
BLEU255
BVAL303
BASP305
BCYN1420

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CYN B 1420
ChainResidue
BGLY256
BTHR260
BHEM1418
BCAM1419
BHOH2342

238895

PDB entries from 2025-07-16

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