Structure of PDB 1pdz Chain A

Receptor sequence

>1pdzA (length=433) Species: 6707 (Homarus gammarus)

SITKVFARTIFDSRGNPTVEVDLYTSKGLFRAAVPSGASTGVHEALEMRD
GDKSKYHGKSVFNAVKNVNDVIVPEIIKSGLKVTQQKECDEFMCKLDGTE
NKSSLGANAILGVSLAICKAGAAELGIPLYRHIANLANYDEVILPVPAFN
VINGGSHAGNKLAMQEFMILPTGATSFTEAMRMGTEVYHHLKAVIKARFG
LDATAVGDEGGFAPNILNNKDALDLIQEAIKKAGYTGKIEIGMDVAASEF
YKQNNIYDLDFKTANNDGSQKISGDQLRDMYMEFCKDFPIVSIEDPFDQD
DWETWSKMTSGTTIQIVGDDLTVTNPKRITTAVEKKACKCLLLKVNQIGS
VTESIDAHLLAKKNGWGTMVSHRSGETEDCFIADLVVGLCTGQIKTGAPC
RSERLAKYNQILRIEEELGSGAKFAGKNFRAPS

3D structure

• PDB: 1pdz X-ray structure and catalytic mechanism of lobster enolase.
• Chain: A
• Resolution: 2.2 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): S39 H157 E166 E209 D244 E294 D319 K344 H372 K395
• Catalytic site (residue number reindexed from 1): S39 H157 E166 E209 D244 E294 D319 K344 H372 K395
• Enzyme Commision number: 4.2.1.11: phosphopyruvate hydratase.

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	PGA	A	S36 K344 R373 S374	S36 K344 R373 S374	MOAD: Ki=0.2mM PDBbind-CN: -logKd/Ki=3.70,Ki=0.2mM
BS02	MN	A	D244 E294 D319	D244 E294 D319

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0004634 phosphopyruvate hydratase activity
• GO:0016829 lyase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0006096 glycolytic process

Cellular Component

• GO:0000015 phosphopyruvate hydratase complex
• GO:0005737 cytoplasm

External links

• PDB: RCSB:1pdz, PDBe:1pdz, PDBj:1pdz
• PDBsum: 1pdz
• PubMed: 7547999
• UniProt: P56252|ENO_HOMGA Enolase