Structure of PDB 4h19 Chain P

Receptor sequence
>4h19P (length=372) Species: 176299 (Agrobacterium fabrum str. C58) [Search protein sequence]
MKITAVEPFILHLPLTSESISDSTHSITHWGVVGAKITTSDGIEGYGFTG
THAHLPSDRLITSCISDCYAPLLLGEDASDHSRLWTKLARYPSLQWVGRA
GITHLALAAVDVALWDIKAKKAGVPLWHYLGGARTAGVEAYNTDIGWLSF
TLEDLLAGSARAVEEDGFTRLKIKVGHDDPNIDIARLTAVRERVDSAVRI
AIDGNGKWDLPTCQRFCAAAKDLDIYWFEEPLWYDDVTSHARLARNTSIP
IALGEQLYTVDAFRSFIDAGAVAYVQPDVTRLGGITEYIQVADLALAHRL
PVVPHAGEMSQVHVHLSYWHPASTILEYIPWIKDHFEEPIHVRDGVYKRP
EQPGASTTPLAESFTRYGKAVK
3D structure
PDB4h19 Crystal structure of an enolase (mandelate racemase subgroup, target EFI-502087) from agrobacterium tumefaciens, with bound Mg and d-ribonohydroxamate, ordered loop
ChainP
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) I20 T51 T143 K172 K174 D203 N205 E229 G254 E255 Q276 D278 H305 A306 G307 E327
Catalytic site (residue number reindexed from 1) I20 T51 T143 K172 K174 D203 N205 E229 G254 E255 Q276 D278 H305 A306 G307 E327
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 CA P D268 H298 D268 H298
BS02 MG P D203 E229 E255 D203 E229 E255
BS03 0YR P D22 H25 H52 K172 K174 D203 E255 H305 E327 D22 H25 H52 K172 K174 D203 E255 H305 E327
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0016836 hydro-lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0016052 carbohydrate catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4h19, PDBe:4h19, PDBj:4h19
PDBsum4h19
PubMed
UniProtQ7CU39

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