Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5IBF

Crystal structure Mycobacterium tuberculosis CYP121 in complex with inhibitor fragment 19a

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 Residues7
Detailsbinding site for residue SO4 A 401
ChainResidue
AARG58
ASER61
AMET62
ALYS63
AHIS343
AHOH501
AHOH502

site_idAC2
Number of Residues22
Detailsbinding site for residue HEM A 402
ChainResidue
AHIS146
APHE230
AGLY234
ASER237
APHE241
APHE280
ALEU284
AARG286
AALA337
APHE338
AGLY339
AGLN342
AHIS343
ACYS345
APRO346
A69W403
AHOH546
AHOH559
AHOH604
AHOH643
AMET62
AMET86

site_idAC3
Number of Residues10
Detailsbinding site for residue 69W A 403
ChainResidue
AVAL78
AVAL82
AVAL83
ASER237
APHE280
AARG386
AHEM402
A69W404
AHOH689
AHOH708

site_idAC4
Number of Residues10
Detailsbinding site for residue 69W A 404
ChainResidue
ATHR77
AVAL78
AALA167
APHE168
AALA178
ATHR229
AGLN385
A69W403
AHOH683
AHOH689

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
ATHR77
ASER237
ALYS301
AGLN385

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
APHE168
ATRP182

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

227344

PDB entries from 2024-11-13

PDB statisticsPDBj update infoContact PDBjnumon