Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2WZD

The catalytically active fully closed conformation of human phosphoglycerate kinase K219A mutant in complex with ADP, 3PG and aluminium trifluoride

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 acetyl-CoA biosynthetic process from pyruvate

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 1417

Chain	Residue
A	ASP374
A	AF31419
A	ADP1420
A	HOH2454
A	HOH2462

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL A 1418

Chain	Residue
A	ARG65
A	LYS215
A	ASP218
A	HOH2254

site_id	AC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE AF3 A 1419

Chain	Residue
A	ARG38
A	LYS215
A	GLY372
A	GLY373
A	GLY395
A	GLY396
A	MG1417
A	ADP1420
A	3PG1421
A	HOH2208
A	HOH2454
A	HOH2462
A	HOH3000

site_id	AC4
Number of Residues	30
Details	BINDING SITE FOR RESIDUE ADP A 1420

Chain	Residue
A	GLY213
A	ALA214
A	LYS215
A	GLY237
A	GLY238
A	LEU256
A	GLY312
A	ASN336
A	PRO338
A	GLY340
A	VAL341
A	GLU343
A	GLY371
A	GLY372
A	GLY373
A	ASP374
A	THR375
A	MG1417
A	AF31419
A	HOH2397
A	HOH2454
A	HOH2455
A	HOH2456
A	HOH2457
A	HOH2458
A	HOH2459
A	HOH2460
A	HOH2461
A	HOH2462
A	HOH3000

site_id	AC5
Number of Residues	15
Details	BINDING SITE FOR RESIDUE 3PG A 1421

Chain	Residue
A	ASP23
A	ASN25
A	ARG38
A	HIS62
A	ARG65
A	ARG122
A	GLY166
A	ARG170
A	LYS215
A	AF31419
A	HOH2462
A	HOH2463
A	HOH2464
A	HOH2465
A	HOH3000

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	ALA219

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	ALA219

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