Structure of PDB 4h8a Chain A

Receptor sequence
>4h8aA (length=337) Species: 562 (Escherichia coli) [Search protein sequence]
MKISRETLHQLIENKLCQAGLKREHAATVAEVLVYADARGIHSHGAVRVE
YYAERISKGGTNREPEFRLEETGPCSAILHADNAAGQVAAKMGMEHAIKT
AQQNGVAVVGISRMGHSGAISYFVQQAARAGFIGISMCQSDPMVVPFGGA
EIYYGTNPLAFAAPGEGDEILTFDMATTVQAWGKVLDARSRNMSIPDTWA
VDKNGVPTTDPFAVHALLPAAGPKGYGLMMMIDVLSGVLLGLPFGRQVSS
MYDDLHAGRNLGQLHIVINPNFFSSSELFRQHLSQTMRELNAITPAPGFN
QVYYPGQDQDIKQRKAAVEGIEIVDDIYQYLISDALY
3D structure
PDB4h8a Structural and functional insights into (s)-ureidoglycolate dehydrogenase, a metabolic branch point enzyme in nitrogen utilization.
ChainA
Resolution1.64 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H44
Catalytic site (residue number reindexed from 1) H44
Enzyme Commision number 1.1.1.350: ureidoglycolate dehydrogenase (NAD(+)).
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 NAI A I41 H44 H116 G118 I120 S140 T156 P158 F173 D174 A176 Y303 G306 D308 Q309 I41 H44 H116 G118 I120 S140 T156 P158 F173 D174 A176 Y303 G306 D308 Q309
BS02 NAI A F147 P223 K224 F147 P223 K224
Gene Ontology
Molecular Function
GO:0009040 ureidoglycolate dehydrogenase activity
GO:0016491 oxidoreductase activity
Biological Process
GO:0000256 allantoin catabolic process
GO:0006144 purine nucleobase metabolic process
GO:0009442 allantoin assimilation pathway
Cellular Component
GO:0005737 cytoplasm

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:4h8a, PDBe:4h8a, PDBj:4h8a
PDBsum4h8a
PubMed23284870
UniProtP77555|ALLD_ECOLI Ureidoglycolate dehydrogenase (NAD(+)) (Gene Name=allD)

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