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4G1X

Crystal structure of Mycobacterium tuberculosis CYP121 in complex with 4-(1H-1,2,4-triazol-1-yl)quinolin-6-amine

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0005737cellular_componentcytoplasm
A0006707biological_processcholesterol catabolic process
A0008395molecular_functionsteroid hydroxylase activity
A0009975molecular_functioncyclase activity
A0016491molecular_functionoxidoreductase activity
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0016717molecular_functionoxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water
A0020037molecular_functionheme binding
A0036199molecular_functioncholest-4-en-3-one 26-monooxygenase activity
A0046872molecular_functionmetal ion binding
A0070025molecular_functioncarbon monoxide binding
Functional Information from PDB Data
site_idAC1
Number of Residues25
DetailsBINDING SITE FOR RESIDUE HEM A 401
ChainResidue
AMET62
AARG286
AALA337
APHE338
AGLY339
AGLN342
AHIS343
ACYS345
APRO346
AGLY347
AGLY351
AMET86
ATQU409
AHOH567
AHOH579
AHOH627
AHOH658
AHOH1147
AHIS146
APHE230
AGLY234
ASER237
ATHR238
APHE280
ALEU284

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 402
ChainResidue
AARG58
ASER61
AMET62
ALYS63
AHIS343
AHOH668
AHOH845
AHOH887
AHOH903
AHOH1239

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 403
ChainResidue
ALYS211
APRO330
AASN331
APRO332
ATHR333
ASER334
AHOH687
AHOH934
AHOH975
AHOH1287

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 404
ChainResidue
ASER219
AARG252
ASER324
AILE325
AHOH654
AHOH796
AHOH880
AHOH891
AHOH1159

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DMS A 405
ChainResidue
APRO19
AASP20
AALA21
AHOH1229

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DMS A 406
ChainResidue
APRO158
AARG162
AHOH624
AHOH827

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE DMS A 407
ChainResidue
APRO316
AASN321
AHOH586
AHOH618
AHOH1041
AHOH1097

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE DMS A 408
ChainResidue
AVAL5
ALYS301

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE TQU A 409
ChainResidue
AASN85
AALA233
ASER237
AARG386
AHEM401
AHOH567
AHOH1074

site_idBC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE TQU A 410
ChainResidue
ATHR77
AVAL78
AALA167
APHE168
ATRP182
AVAL228
ATHR229
AGLY232
AHOH603
AHOH616
AHOH700
AHOH1072
AHOH1075
AHOH1127

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGrGQHFCPG
ChainResidueDetails
APHE338-GLY347

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:17028183, ECO:0000269|PubMed:19416919
ChainResidueDetails
ASER237
ALYS301
AGLN385
ATHR77

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING:
ChainResidueDetails
AASN85

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:12435731, ECO:0000269|PubMed:17028183, ECO:0000269|PubMed:18818197, ECO:0000269|PubMed:19416919, ECO:0000269|PubMed:22890978, ECO:0000269|PubMed:23620594
ChainResidueDetails
AARG286
AHIS343

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: axial binding residue
ChainResidueDetails
ACYS345

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Participates in a stacking interactions with the tyrosyl of cYY
ChainResidueDetails
ATRP182
APHE168

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Important for the position of heme
ChainResidueDetails
APRO346

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PDB entries from 2024-06-12

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