Structure of PDB 3erp Chain A

Receptor sequence
>3erpA (length=312) Species: 99287 (Salmonella enterica subsp. enterica serovar Typhimurium str. LT2) [Search protein sequence]
IYQPDENRYHTMEYRRCGRSGVKLPAISLGLWHNFGDTTRVENSRALLQR
AFDLGITHFDLANNYGPPPGSAECNFGRILQEDFLPWRDELIISTKAGYT
MWDGPYGDWGSRKYLIASLDQSLKRMGLEYVDIFYHHRPDPETPLKETMK
ALDHLVRHGKALYVGISNYPADLARQAIDILEDLGTPCLIHQPKYSLFER
WVEDGLLALLQEKGVGSIAFSPLAGGQLTDRYLNITADKLEKVRRLNELA
ARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQIEDAVGMLANRRFSAAE
CAEIDAILEGRF
3D structure
PDB3erp Structural and biochemical studies of novel aldo-keto reductases for the biocatalytic conversion of 3-hydroxybutanal to 1,3-butanediol.
ChainA
Resolution1.55 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 CAC A W33 Y66 H138 F221 W32 Y65 H137 F220
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
Biological Process
GO:0051596 methylglyoxal catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3erp, PDBe:3erp, PDBj:3erp
PDBsum3erp
PubMed28130301
UniProtQ8ZNA1

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