2PAA

Crystal structure of phosphoglycerate kinase-2 bound to atp 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	0005929	cellular_component	cilium
A	0006094	biological_process	gluconeogenesis
A	0006096	biological_process	glycolytic process
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0030317	biological_process	flagellated sperm motility
A	0035686	cellular_component	sperm fibrous sheath
A	0043531	molecular_function	ADP binding
A	0046872	molecular_function	metal ion binding
B	0000166	molecular_function	nucleotide binding
B	0004618	molecular_function	phosphoglycerate kinase activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005929	cellular_component	cilium
B	0006094	biological_process	gluconeogenesis
B	0006096	biological_process	glycolytic process
B	0016301	molecular_function	kinase activity
B	0016740	molecular_function	transferase activity
B	0030317	biological_process	flagellated sperm motility
B	0035686	cellular_component	sperm fibrous sheath
B	0043531	molecular_function	ADP binding
B	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ATP A 500

Chain	Residue
A	GLY212
A	ASN336
A	GLY337
A	PRO338
A	GLY340
A	VAL341
A	GLU343
A	GLY373
A	ASP374
A	THR375
A	GLY213
A	ALA214
A	LYS219
A	GLY237
A	GLY238
A	LEU256
A	GLY312
A	LEU313

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE 3PG B 501

Chain	Residue
B	HIS62
B	ARG122
B	GLY166
B	ARG170

---

Functional Information from PROSITE/UniProt

site_id	PS00111
Number of Residues	11
Details	PGLYCERATE_KINASE Phosphoglycerate kinase signature. RVIMRvDfNVP

Chain	Residue	Details
A	ARG17-PRO27

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	28
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P00558","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18004764","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2P9T","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18004764","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2P9T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PAA","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q7SIB7","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18004764","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2PAA","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	20
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P00558","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P00558","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

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

---

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 13pk

Chain	Residue	Details
B	ARG38
B	LYS215
B	GLY396

---