1KF0

Crystal Structure of Pig Muscle Phosphoglycerate Kinase Ternary Complex with AMP-PCP and 3PG

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
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	0016740	molecular_function	transferase activity
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 518

Chain	Residue
A	ASP218
A	ACP418

---

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 3PG A 417

Chain	Residue
A	ARG170
A	HOH451
A	HOH476
A	HOH500
A	ASP23
A	ASN25
A	ARG38
A	HIS62
A	ARG65
A	ARG122
A	GLY166

---

site_id	AC3
Number of Residues	16
Details	BINDING SITE FOR RESIDUE ACP A 418

Chain	Residue
A	GLY213
A	ALA214
A	LYS215
A	LYS219
A	GLY237
A	GLY238
A	PHE241
A	GLY312
A	GLY340
A	VAL341
A	GLU343
A	ASP374
A	HOH426
A	HOH467
A	HOH506
A	MG518

---

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	PHE24
A	ILE39
A	LEU63
A	PHE123
A	ALA171

---

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

Chain	Residue	Details
A	ILE220
A	LEU313
A	TRP344
A	GLY373

---

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

Chain	Residue	Details
A	LEU2
A	ASN4
A	PRO203

---

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

Chain	Residue	Details
A	LEU6
A	LYS191

---

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

Chain	Residue	Details
A	LEU11
A	TYR75
A	SER86
A	ILE146
A	ALA199
A	ASN267
A	PHE291

---

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	ASP91
A	ALA361

---

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	VAL216
A	ILE220
A	TYR323

---