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4ZAL

Structure of UbiX E49Q mutant in complex with reduced FMN and dimethylallyl monophosphate

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004659molecular_functionprenyltransferase activity
A0016740molecular_functiontransferase activity
A0016831molecular_functioncarboxy-lyase activity
A0106141molecular_functionflavin prenyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue 4LR A 301
ChainResidue
ATRP84
AARG185
ATRP200
AFNR302
AHOH435
AALA89
ASER90
AGLY91
AARG122
ALYS129
AARG139
AGLU140
ATYR169

site_idAC2
Number of Residues21
Detailsbinding site for residue FNR A 302
ChainResidue
ATHR12
AGLY13
AALA14
ASER15
ASER39
AALA41
AGLN49
ATRP84
ASER104
ATHR105
ATHR107
ACYS116
AARG122
AARG139
A4LR301
AHOH424
AHOH442
AHOH452
AHOH455
AHOH470
AHOH471

site_idAC3
Number of Residues2
Detailsbinding site for residue SCN A 303
ChainResidue
AGLU31
AGLU33

site_idAC4
Number of Residues3
Detailsbinding site for residue SCN A 304
ChainResidue
AARG131
AARG132
AHOH504

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
AGLY13
ASER39
ASER104
ACYS116
AARG139

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01984, ECO:0000269|PubMed:26083743
ChainResidueDetails
ATYR169
AARG185

237423

PDB entries from 2025-06-11

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