Structure of PDB 4e4f Chain D

Receptor sequence
>4e4fD (length=388) Species: 561230 (Pectobacterium carotovorum subsp. carotovorum PC1) [Search protein sequence]
FQSMKIVSAEVFVTCPGRNFVTLKITTDSGLTGLGDATLNGRELPVASYL
NDHVCPQLIGRDAHQIEDIWQYFYKGAYWRRGPVTMSAISAVDMALWDIK
AKAANMPLYQLLGGASRTGVMVYCHTTGHSIDEVLDDYAKHRDQGFKAIR
VQCEPATKGSLPEEQLWSTEKYLDFTPKLFEAVRDKFGFNEHLLHDMHHR
LTPIEAARFGKSVEDYRLFWMEDPTPAENQACFRLIRQHTVTPIAVGEVF
NSIWDCKQLIEEQLIDYIRTTITHAGGITGMRRIADFASLYQVRTGSHGP
SDLSPICMAAALHFDLWVPNFGVQEYMGYSEQMLEVFPHSWTFDNGYMHP
GEKPGLGIEFDEKLAAKYPYDPAYLPVARLEDGTLWNW
3D structure
PDB4e4f Crystal structure of ENOLASE PC1_0802 from Pectobacterium carotovorum
ChainD
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L36 R39 R147 Q149 D212 H214 E238 G263 E264 V265 R285 T287 H314 P316 E341 W404
Catalytic site (residue number reindexed from 1) L39 R42 R150 Q152 D196 H198 E222 G247 E248 V249 R269 T271 H298 P300 E325 W388
Enzyme Commision number 4.2.1.-
4.2.1.8: mannonate dehydratase.
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 D D212 E238 E264 D196 E222 E248
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0008927 mannonate dehydratase activity
GO:0016829 lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0009063 amino acid catabolic process
GO:0016052 carbohydrate catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4e4f, PDBe:4e4f, PDBj:4e4f
PDBsum4e4f
PubMed
UniProtC6D9S0|MAND_PECCP D-galactonate dehydratase family member PC1_0802 (Gene Name=PC1_0802)

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