Structure of PDB 2x15 Chain A

Receptor sequence

>2x15A (length=408) Species: 9606 (Homo sapiens) [Search protein sequence]

LSNKLTLDKLDVKGKRVVMRVDFNVPMKNNQITNNQRIKAAVPSIKFCLD
NGAKSVVLMSHLGRPDGVPMPDKYSLEPVAVELKSLLGKDVLFLKDCVGP
EVEKACANPAAGSVILLENLRFHVEEEGKGKKAEPAKIEAFRASLSKLGD
VYVNDAFGTAHRAHSSMVGVNLPQKAGGFLMKKELNYFAKALESPERPFL
AILGGAKVADKIQLINNMLDKVNEMIIGGGMAFTFLKVLNNMEIGTSLFD
EEGAKIVKDLMSKAEKNGVKITLPVDFVTADKFDENAKTGQATVASGIPA
GWMGLDCGPESSKKYAEAVTRAKQIVWNGPVGVFEWEAFARGTKALMDEV
VKATSRGCITIIGGGDTATCCAKWNTEDKVSHVSTGGGASLELLEGKVLP
GVDALSNI

3D structure

PDB

2x15 The Structure of Human Phosphoglycerate Kinase in its Fully Active Conformation in Complex with Ground State Analoges

Chain

Resolution

2.1 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	R39 K216 G374 G397
Catalytic site (residue number reindexed from 1)	R37 K207 G365 G388
Enzyme Commision number	2.7.2.3: phosphoglycerate kinase.

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)
BS01	ADP	A	G214 A215 K216 K220 G238 G239 N337 P339 G341 V342 E344 G373 G374 D375 T376	G205 A206 K207 K211 G229 G230 N328 P330 G332 V333 E335 G364 G365 D366 T367
BS02	X15	A	D24 N26 R39 H63 R66 R123 R171 K216 K220 G373 G396 G397	D22 N24 R37 H61 R64 R121 R162 K207 K211 G364 G387 G388
BS03	ATP	A	G214 A215 K216 K220 G238 G239 N337 G341 V342 E344 G373 G374 D375 T376 G396 G397	G205 A206 K207 K211 G229 G230 N328 G332 V333 E335 G364 G365 D366 T367 G387 G388

Gene Ontology

	Molecular Function
GO:0004618	phosphoglycerate kinase activity
GO:0005515	protein binding
GO:0005524	ATP binding
GO:0016301	kinase activity
GO:0043531	ADP binding
GO:0047134	protein-disulfide reductase (NAD(P)H) activity

	Biological Process
GO:0006094	gluconeogenesis
GO:0006096	glycolytic process
GO:0016310	phosphorylation
GO:0016525	negative regulation of angiogenesis
GO:0030855	epithelial cell differentiation
GO:0031639	plasminogen activation
GO:0061621	canonical glycolysis
GO:0071456	cellular response to hypoxia

	Cellular Component
GO:0005615	extracellular space
GO:0005737	cytoplasm
GO:0005829	cytosol
GO:0016020	membrane
GO:0045121	membrane raft
GO:0070062	extracellular exosome

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Molecular Function

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Biological Process

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Cellular Component

External links

PDB	RCSB:2x15, PDBe:2x15, PDBj:2x15
PDBsum	2x15
PubMed
UniProt	P00558\|PGK1_HUMAN Phosphoglycerate kinase 1 (Gene Name=PGK1)

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