1HDI

Pig muscle 3-PHOSPHOGLYCERATE KINASE complexed with 3-PG and MgADP.

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	2
Details	BINDING SITE FOR RESIDUE MG A 418

Chain	Residue
A	ASP374
A	AMP417

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site_id	AC2
Number of Residues	21
Details	BINDING SITE FOR RESIDUE AMP A 417

Chain	Residue
A	LEU313
A	GLY340
A	VAL341
A	GLU343
A	ASP374
A	MG418
A	HOH2111
A	HOH2182
A	HOH2201
A	HOH2202
A	HOH2203
A	HOH2204
A	HOH2205
A	HOH2206
A	ALA214
A	LYS215
A	LYS219
A	GLY237
A	GLY238
A	LEU256
A	GLY312

---

site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 3PG A 419

Chain	Residue
A	ASP23
A	ASN25
A	ARG38
A	HIS62
A	ARG65
A	ARG122
A	GLY166
A	ARG170
A	HOH2009
A	HOH2207
A	HOH2208

---

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	ASP23
A	ARG38
A	HIS62
A	ARG122
A	ARG170

---

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

Chain	Residue	Details
A	LYS219
A	GLY312
A	GLU343
A	GLY372

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P09411

Chain	Residue	Details
A	LYS5
A	LYS190

---

site_id	SWS_FT_FI4
Number of Residues	7
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P00558

Chain	Residue	Details
A	LYS10
A	LYS74
A	LYS85
A	LYS145
A	ALA198
A	LYS266
A	LYS290

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P09411

Chain	Residue	Details
A	LYS47

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P09411

Chain	Residue	Details
A	TYR75

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P09411

Chain	Residue	Details
A	LYS90
A	LYS360

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P00558

Chain	Residue	Details
A	LYS96

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: N6-malonyllysine; alternate => ECO:0000250

Chain	Residue	Details
A	LYS130

---

site_id	SWS_FT_FI10
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P00558

Chain	Residue	Details
A	TYR195

---

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

Chain	Residue	Details
A	SER202

---

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

Chain	Residue	Details
A	LYS215
A	LYS219
A	LYS322

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 13pk

Chain	Residue	Details
A	ARG38
A	LYS215
A	GLY373
A	GLY396

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