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5WP2

1.44 Angstrom crystal structure of CYP121 from Mycobacterium tuberculosis in complex with substrate and CN

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 Residues24
Detailsbinding site for residue HEM A 401
ChainResidue
AMET62
AARG286
AALA337
APHE338
AGLY339
AHIS343
ACYS345
APRO346
AGLY347
AYTT402
ACYN403
AMET86
AHOH507
AHOH580
AHOH595
AHOH607
AHOH625
AHIS146
APHE230
AGLY234
ASER237
ATHR238
APHE280
ALEU284

site_idAC2
Number of Residues15
Detailsbinding site for residue YTT A 402
ChainResidue
AVAL78
AVAL82
AVAL83
AASN85
AALA167
APHE168
ATHR229
AARG386
AHEM401
ACYN403
AHOH533
AHOH580
AHOH586
AHOH687
AHOH830

site_idAC3
Number of Residues5
Detailsbinding site for residue CYN A 403
ChainResidue
AALA233
ASER237
AARG386
AHEM401
AYTT402

site_idAC4
Number of Residues7
Detailsbinding site for residue SO4 A 404
ChainResidue
ASER12
AHOH510
AHOH554
AHOH587
AHOH634
AHOH702
AHOH705

site_idAC5
Number of Residues8
Detailsbinding site for residue SO4 A 405
ChainResidue
AARG58
ASER61
AMET62
ALYS63
AHIS343
AHOH505
AHOH512
AHOH537

site_idAC6
Number of Residues8
Detailsbinding site for residue SO4 A 406
ChainResidue
ALYS211
APRO330
AASN331
APRO332
ATHR333
ASER334
AHOH503
AHOH707

site_idAC7
Number of Residues4
Detailsbinding site for residue SO4 A 407
ChainResidue
APRO158
AARG162
AHOH518
AHOH693

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
APHE168
ATRP182

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

221051

PDB entries from 2024-06-12

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