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6N6Q

Crystal structure of a Cytochrome P450 (CYP102L1)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
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
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0020037molecular_functionheme binding
B0046872molecular_functionmetal ion binding
C0004497molecular_functionmonooxygenase activity
C0005506molecular_functioniron ion binding
C0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
C0020037molecular_functionheme binding
C0046872molecular_functionmetal ion binding
D0004497molecular_functionmonooxygenase activity
D0005506molecular_functioniron ion binding
D0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
D0020037molecular_functionheme binding
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues25
Detailsbinding site for residue HEM A 501
ChainResidue
ALYS90
ASER294
AVAL355
AALA356
ATYR359
APRO422
AGLY424
AARG428
AALA429
ACYS430
AILE431
AMET107
AALA436
AHOH610
AHOH612
AHOH617
AHOH618
AHOH633
APHE108
ATRP117
APHE128
APHE286
AALA289
AGLY290
ATHR293

site_idAC2
Number of Residues5
Detailsbinding site for residue CAC A 502
ChainResidue
ATYR111
AASN112
ASER113
AGLN362
AHOH608

site_idAC3
Number of Residues21
Detailsbinding site for residue HEM B 501
ChainResidue
BLYS90
BLEU96
BMET107
BPHE108
BTRP117
BILE175
BALA289
BGLY290
BTHR293
BSER294
BTYR359
BPRO422
BPHE423
BGLY424
BARG428
BALA429
BCYS430
BILE431
BGLY432
BALA436
BHOH604

site_idAC4
Number of Residues5
Detailsbinding site for residue CAC B 502
ChainResidue
BGLU89
BTYR111
BASN112
BSER113
BGLN362

site_idAC5
Number of Residues5
Detailsbinding site for residue CAC B 503
ChainResidue
BGLY30
BGLY30
BARG31
BARG31
BLEU32

site_idAC6
Number of Residues22
Detailsbinding site for residue HEM C 501
ChainResidue
CLYS90
CMET107
CPHE108
CTRP117
CALA289
CGLY290
CTHR293
CSER294
CVAL355
CTYR359
CPRO422
CPHE423
CGLY424
CARG428
CALA429
CCYS430
CALA436
CHOH603
CHOH604
CHOH607
CHOH611
CHOH615

site_idAC7
Number of Residues6
Detailsbinding site for residue CAC C 502
ChainResidue
CGLU89
CTYR111
CASN112
CSER113
CGLN362
CHOH606

site_idAC8
Number of Residues25
Detailsbinding site for residue HEM D 501
ChainResidue
DALA356
DTYR359
DPRO422
DPHE423
DGLY424
DARG428
DALA429
DCYS430
DILE431
DALA436
DGLU439
DHOH602
DHOH605
DHOH607
DHOH611
DLYS90
DMET107
DPHE108
DTRP117
DPHE128
DILE175
DALA289
DGLY290
DTHR293
DSER294

site_idAC9
Number of Residues4
Detailsbinding site for residue CAC D 502
ChainResidue
DTYR111
DASN112
DSER113
DGLN362

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGvGERACIG
ChainResidueDetails
APHE423-GLY432

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PDB entries from 2024-07-31

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