Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2Y3I

The structure of the fully closed conformation of human PGK in complex with L-ADP, 3PG and the TSA aluminium tetrafluoride

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004618	molecular_function	phosphoglycerate kinase activity
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005576	cellular_component	extracellular region
A	0005759	cellular_component	mitochondrial matrix
A	0005829	cellular_component	cytosol
A	0006094	biological_process	gluconeogenesis
A	0006096	biological_process	glycolytic process
A	0016020	cellular_component	membrane
A	0016525	biological_process	negative regulation of angiogenesis
A	0030855	biological_process	epithelial cell differentiation
A	0031639	biological_process	plasminogen activation
A	0043531	molecular_function	ADP binding
A	0044325	molecular_function	transmembrane transporter binding
A	0045121	cellular_component	membrane raft
A	0047134	molecular_function	protein-disulfide reductase [NAD(P)H] activity
A	0061621	biological_process	canonical glycolysis
A	0070062	cellular_component	extracellular exosome
A	0071456	biological_process	cellular response to hypoxia
A	0106310	molecular_function	protein serine kinase activity
A	0160218	biological_process	negative regulation of pyruvate decarboxylation to acetyl-CoA
D	0004618	molecular_function	phosphoglycerate kinase activity
D	0004674	molecular_function	protein serine/threonine kinase activity
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005576	cellular_component	extracellular region
D	0005759	cellular_component	mitochondrial matrix
D	0005829	cellular_component	cytosol
D	0006094	biological_process	gluconeogenesis
D	0006096	biological_process	glycolytic process
D	0016020	cellular_component	membrane
D	0016525	biological_process	negative regulation of angiogenesis
D	0030855	biological_process	epithelial cell differentiation
D	0031639	biological_process	plasminogen activation
D	0043531	molecular_function	ADP binding
D	0044325	molecular_function	transmembrane transporter binding
D	0045121	cellular_component	membrane raft
D	0047134	molecular_function	protein-disulfide reductase [NAD(P)H] activity
D	0061621	biological_process	canonical glycolysis
D	0070062	cellular_component	extracellular exosome
D	0071456	biological_process	cellular response to hypoxia
D	0106310	molecular_function	protein serine kinase activity
D	0160218	biological_process	negative regulation of pyruvate decarboxylation to acetyl-CoA

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A 1416

Chain	Residue
A	ASP374
A	LA81418
A	ALF1419

site_id	AC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE LA8 D 1416

Chain	Residue
D	GLY340
D	GLU343
D	GLY372
D	GLY373
D	ASP374
D	THR375
D	ALF1417
D	MG1418
D	GLY213
D	ALA214
D	LYS215
D	LYS219
D	ASN336
D	PRO338

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL A 1417

Chain	Residue
A	LYS215
A	ALA217
A	ASP218

site_id	AC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE ALF D 1417

Chain	Residue
D	ARG38
D	LYS215
D	LYS219
D	GLY372
D	GLY373
D	GLY395
D	GLY396
D	LA81416
D	MG1418
D	3PG1420
D	HOH2005

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG D 1418

Chain	Residue
D	ASP374
D	LA81416
D	ALF1417

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL D 1419

Chain	Residue
D	ARG65
D	LYS215
D	ASP218

site_id	AC7
Number of Residues	18
Details	BINDING SITE FOR RESIDUE LA8 A 1418

Chain	Residue
A	GLY213
A	ALA214
A	LYS215
A	LYS219
A	PHE291
A	ASN336
A	PRO338
A	GLY340
A	VAL341
A	PHE342
A	GLU343
A	GLY372
A	GLY373
A	ASP374
A	THR375
A	MG1416
A	ALF1419
A	HOH2008

site_id	AC8
Number of Residues	11
Details	BINDING SITE FOR RESIDUE ALF A 1419

Chain	Residue
A	ARG38
A	LYS215
A	LYS219
A	GLY372
A	GLY373
A	ASP374
A	GLY395
A	GLY396
A	MG1416
A	LA81418
A	3PG1420

site_id	AC9
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 3PG D 1420

Chain	Residue
D	ASP23
D	ASN25
D	ARG38
D	HIS62
D	ARG65
D	ARG122
D	GLY166
D	ARG170
D	LYS215
D	ALF1417
D	HOH2005

site_id	BC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE 3PG A 1420

Chain	Residue
A	ASP23
A	ASN25
A	ARG38
A	HIS62
A	ARG65
A	ARG122
A	GLY166
A	ARG170
A	LYS215
A	ALF1419

Functional Information from PROSITE/UniProt

site_id	PS00111
Number of Residues	11
Details	PGLYCERATE_KINASE Phosphoglycerate kinase signature. RVVMRvDfNVP

Chain	Residue	Details
A	ARG17-PRO27

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	10
Details	Region: {"description":"Mitochondrial targeting region exposed following cis-trans isomerization by PIN1 and recognized by the TOM complex for mitochondrial translocation of the protein","evidences":[{"source":"PubMed","id":"26942675","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18463139","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3C39","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3C3A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3C3C","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	28
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q7SIB7","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18463139","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3C39","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3C3C","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18463139","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3C3B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3C3C","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18463139","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3C3A","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18463139","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3C3A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3C3C","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18463139","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3C3B","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18463139","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3C3C","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	4
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P09411","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	14
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P09411","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P09411","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P09411","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	2
Details	Modified residue: {"description":"N6-malonyllysine; alternate","evidences":[{"source":"PubMed","id":"21908771","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine; by MAPK1","evidences":[{"source":"PubMed","id":"26942675","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17081983","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	4
Details	Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"PubMed","id":"29775581","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	2
Details	Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"PubMed","id":"29192674","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)