1VJC

Structure of pig muscle PGK complexed with MgATP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004618	molecular_function	phosphoglycerate kinase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006094	biological_process	gluconeogenesis
A	0006096	biological_process	glycolytic process
A	0016301	molecular_function	kinase activity
A	0016310	biological_process	phosphorylation
A	0043531	molecular_function	ADP binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE MG A 418

Chain	Residue
A	ATP417

---

site_id	AC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ATP A 417

Chain	Residue
A	VAL341
A	GLU343
A	ASP374
A	MG418
A	HOH455
A	HOH465
A	HOH470
A	HOH543
A	HOH545
A	GLY213
A	ALA214
A	LYS219
A	GLY237
A	GLY238
A	LEU256
A	GLY312
A	GLY340

---

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:11178909

Chain	Residue	Details
A	ILE39
A	LEU63
A	PHE123
A	ALA171
A	PHE24

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:15035615

Chain	Residue	Details
A	GLY373
A	ILE220
A	LEU313
A	TRP344

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00558

Chain	Residue	Details
A	PRO203
A	LEU2
A	ASN4

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P09411

Chain	Residue	Details
A	LYS191
A	LEU6

---

site_id	SWS_FT_FI5
Number of Residues	7
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P00558

Chain	Residue	Details
A	ILE146
A	ALA199
A	ASP267
A	PHE291
A	LEU11
A	TYR75
A	SER86

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P09411

Chain	Residue	Details
A	PHE48

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P09411

Chain	Residue	Details
A	SER76

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P09411

Chain	Residue	Details
A	ALA361
A	ASP91

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P00558

Chain	Residue	Details
A	ASP97

---

site_id	SWS_FT_FI10
Number of Residues	1
Details	MOD_RES: N6-malonyllysine; alternate => ECO:0000250

Chain	Residue	Details
A	GLY131

---

site_id	SWS_FT_FI11
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P00558

Chain	Residue	Details
A	PHE196

---

site_id	SWS_FT_FI12
Number of Residues	3
Details	MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P00558

Chain	Residue	Details
A	ILE220
A	TYR323
A	VAL216

---