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4ZAZ

Structure of UbiX Y169F in complex with a covalent adduct formed between reduced FMN and dimethylallyl monophosphate

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004659molecular_functionprenyltransferase activity
A0016831molecular_functioncarboxy-lyase activity
A0106141molecular_functionflavin prenyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues23
Detailsbinding site for residue 4LS A 301
ChainResidue
ATHR12
ASER104
ATHR105
ATHR107
ACYS116
AARG122
AARG139
ATRP200
APO4306
AHOH448
AHOH461
AGLY13
AHOH497
AHOH509
AHOH514
AHOH516
AALA14
ASER15
ASER39
AALA41
AVAL45
ATRP84
AALA89

site_idAC2
Number of Residues9
Detailsbinding site for residue SCN A 302
ChainResidue
AGLN62
ATHR66
AALA71
AALA72
AGLY74
AGLN75
AILE76
AHOH401
AHOH457

site_idAC3
Number of Residues3
Detailsbinding site for residue SCN A 303
ChainResidue
AGLN59
AHOH444
AHOH499

site_idAC4
Number of Residues3
Detailsbinding site for residue SCN A 304
ChainResidue
AASN96
AALA97
APRO133

site_idAC5
Number of Residues3
Detailsbinding site for residue NA A 305
ChainResidue
ALYS40
AHOH404
AHOH552

site_idAC6
Number of Residues10
Detailsbinding site for residue PO4 A 306
ChainResidue
ASER90
AGLY91
AARG122
ALYS129
AARG139
AGLU140
APHE169
AARG185
A4LS301
AHOH406

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01984, ECO:0000269|PubMed:22102023
ChainResidueDetails
ASER104
ACYS116
AARG139
AGLY13
ASER39

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01984, ECO:0000269|PubMed:26083743
ChainResidueDetails
APHE169
AARG185

219869

PDB entries from 2024-05-15

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