Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2XE8

The complete reaction cycle of human phosphoglycerate kinase: The open ternary complex with 3PG and AMP-PNP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
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	0005615	cellular_component	extracellular space
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
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	0016301	molecular_function	kinase activity
A	0016525	biological_process	negative regulation of angiogenesis
A	0016740	molecular_function	transferase activity
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	0046872	molecular_function	metal ion binding
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

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE 3PG A 1417

Chain	Residue
A	ASP23
A	HOH2140
A	ASN25
A	ARG38
A	HIS62
A	ARG65
A	ARG122
A	GLY166
A	ARG170
A	HOH2061

site_id	AC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE ACP A 1418

Chain	Residue
A	GLY213
A	ALA214
A	GLY237
A	GLY238
A	LEU256
A	GLY312
A	LEU313
A	GLY340
A	VAL341
A	GLU343
A	ASP374
A	HOH2107
A	HOH2118
A	HOH2119

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	5
Details	BINDING: BINDING => ECO:0000269\|PubMed:18463139, ECO:0007744\|PDB:3C39, ECO:0007744\|PDB:3C3A, ECO:0007744\|PDB:3C3C

Chain	Residue	Details
A	VAL22
A	PHE24
A	GLN37
A	LEU121
A	HIS169

site_id	SWS_FT_FI2
Number of Residues	14
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:Q7SIB7

Chain	Residue	Details
A	ASP23
A	GLY238
A	GLY312
A	GLU343
A	ASP374
A	THR375
A	ASN25
A	ARG38
A	HIS62
A	ARG65
A	ARG122
A	ARG170
A	LYS215
A	LYS219

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:18463139, ECO:0007744\|PDB:3C39, ECO:0007744\|PDB:3C3C

Chain	Residue	Details
A	SER61
A	GLY64

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269\|PubMed:18463139, ECO:0007744\|PDB:3C3B, ECO:0007744\|PDB:3C3C

Chain	Residue	Details
A	GLY213

site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:18463139, ECO:0007744\|PDB:3C3A

Chain	Residue	Details
A	ALA214
A	ASP218

site_id	SWS_FT_FI6
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269\|PubMed:18463139, ECO:0007744\|PDB:3C3A, ECO:0007744\|PDB:3C3C

Chain	Residue	Details
A	ALA217

site_id	SWS_FT_FI7
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:18463139, ECO:0007744\|PDB:3C3B

Chain	Residue	Details
A	GLY237
A	GLY337

site_id	SWS_FT_FI8
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:18463139, ECO:0007744\|PDB:3C3C

Chain	Residue	Details
A	VAL339
A	PHE342

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
A	SER1
A	SER3

site_id	SWS_FT_FI10
Number of Residues	2
Details	MOD_RES: N6-succinyllysine => ECO:0000250\|UniProtKB:P09411

Chain	Residue	Details
A	LYS5
A	LYS190

site_id	SWS_FT_FI11
Number of Residues	7
Details	MOD_RES: N6-acetyllysine => ECO:0007744\|PubMed:19608861

Chain	Residue	Details
A	LYS10
A	LYS74
A	LYS85
A	LYS145
A	LYS198
A	LYS266
A	LYS290

site_id	SWS_FT_FI12
Number of Residues	1
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250\|UniProtKB:P09411

Chain	Residue	Details
A	LYS47

site_id	SWS_FT_FI13
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000250\|UniProtKB:P09411

Chain	Residue	Details
A	TYR75

site_id	SWS_FT_FI14
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:P09411

Chain	Residue	Details
A	LYS90
A	LYS360

site_id	SWS_FT_FI15
Number of Residues	1
Details	MOD_RES: N6-acetyllysine; alternate => ECO:0007744\|PubMed:19608861

Chain	Residue	Details
A	LYS96

site_id	SWS_FT_FI16
Number of Residues	1
Details	MOD_RES: N6-malonyllysine; alternate => ECO:0000269\|PubMed:21908771

Chain	Residue	Details
A	LYS130

site_id	SWS_FT_FI17
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0007744\|PubMed:15592455

Chain	Residue	Details
A	TYR195

site_id	SWS_FT_FI18
Number of Residues	1
Details	MOD_RES: Phosphoserine; by MAPK1 => ECO:0000269\|PubMed:26942675, ECO:0007744\|PubMed:17081983, ECO:0007744\|PubMed:20068231, ECO:0007744\|PubMed:21406692, ECO:0007744\|PubMed:23186163, ECO:0007744\|PubMed:24275569

Chain	Residue	Details
A	SER202

site_id	SWS_FT_FI19
Number of Residues	2
Details	MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269\|PubMed:29775581

Chain	Residue	Details
A	LYS215
A	LYS322

site_id	SWS_FT_FI20
Number of Residues	1
Details	MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269\|PubMed:29192674

Chain	Residue	Details
A	LYS219

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