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4C9O

Structure of Cyanide and Camphor bound D259N mutant of 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 Residues19
DetailsBINDING SITE FOR RESIDUE HEM A 422
ChainResidue
ATHR103
AARG307
ATHR357
AALA359
AHIS363
ACYS365
AGLY367
AALA371
ACAM423
ACYN424
AHOH2191
AHIS110
AARG114
APHE165
ALEU253
AGLY257
ATHR260
APHE264
AASP305

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CAM A 423
ChainResidue
ATRP89
ATYR98
ATHR103
ALEU255
AVAL303
AASP305
AHEM422
ACYN424

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CYN A 424
ChainResidue
AGLY256
ATHR260
AHEM422
ACAM423

site_idAC4
Number of Residues21
DetailsBINDING SITE FOR RESIDUE HEM B 422
ChainResidue
BPRO102
BTHR103
BHIS110
BARG114
BPHE165
BLEU253
BGLY257
BTHR260
BVAL261
BPHE264
BPHE297
BASP305
BARG307
BTHR357
BPRO362
BHIS363
BCYS365
BGLY367
BCAM423
BCYN424
BHOH2148

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CAM B 423
ChainResidue
BTRP89
BTYR98
BLEU255
BVAL303
BASP305
BHEM422
BCYN424

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CYN B 424
ChainResidue
BGLY256
BTHR260
BHEM422
BCAM423

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PDB entries from 2024-10-09

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