Structure of PDB 1rya Chain A

Receptor sequence
>1ryaA (length=160) Species: 562 (Escherichia coli) [Search protein sequence]
MMFLRQEDFATVVRSTPLVSLDFIVENSRGEFLLGKRTNRPAQGYWFVPG
GRVQKDETLEAAFERLTMAELGLRLPITAGQFYGVWQHFYDDNFSGTDFT
THYVVLGFRFRVSEEELLLPDEQHDDYRWLTSDALLASDNVHANSRAYFL
AEKRTGVPGL
3D structure
PDB1rya Structure and mechanism of GDP-mannose glycosyl hydrolase, a Nudix enzyme that cleaves at carbon instead of phosphorus.
ChainA
Resolution1.3 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.6.1.-
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 MG A G50 E70 Q123 G50 E70 Q123
BS02 GDP A F3 L4 F9 R37 N39 G50 G51 R52 Y103 Q123 F3 L4 F9 R37 N39 G50 G51 R52 Y103 Q123
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0008727 GDP-mannose mannosyl hydrolase activity
GO:0016787 hydrolase activity
GO:0030145 manganese ion binding
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
GO:0047917 GDP-glucosidase activity
Biological Process
GO:0009103 lipopolysaccharide biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1rya, PDBe:1rya, PDBj:1rya
PDBsum1rya
PubMed15274914
UniProtP32056|GMM_ECOLI GDP-mannose mannosyl hydrolase (Gene Name=gmm)

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