2P9Q

Crystal Structure of Phosphoglycerate Kinase-2

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 PROSITE/UniProt

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

Chain	Residue	Details
A	ARG17-PRO27

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	28
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P00558

Chain	Residue	Details
A	VAL22
A	ASP218
A	GLY237
A	GLY337
A	ILE339
A	PHE342
B	VAL22
B	PHE24
B	GLN37
B	SER61
B	GLY64
A	PHE24
B	LEU121
B	HIS169
B	GLY213
B	ALA214
B	ASP218
B	GLY237
B	GLY337
B	ILE339
B	PHE342
A	GLN37
A	SER61
A	GLY64
A	LEU121
A	HIS169
A	GLY213
A	ALA214

---

site_id	SWS_FT_FI2
Number of Residues	10
Details	BINDING: BINDING => ECO:0000269|PubMed:18004764, ECO:0007744|PDB:2P9T

Chain	Residue	Details
A	ASP23
B	ARG170
A	ASN25
A	ARG38
A	ARG65
A	ARG170
B	ASP23
B	ASN25
B	ARG38
B	ARG65

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:18004764, ECO:0007744|PDB:2P9T, ECO:0007744|PDB:2PAA

Chain	Residue	Details
A	HIS62
A	ARG122
B	HIS62
B	ARG122

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q7SIB7

Chain	Residue	Details
A	LYS215
A	ASP374
A	THR375
B	LYS215
B	ASP374
B	THR375

---

site_id	SWS_FT_FI5
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:18004764, ECO:0007744|PDB:2PAA

Chain	Residue	Details
A	LYS219
A	GLY238
A	GLY312
A	GLU343
B	LYS219
B	GLY238
B	GLY312
B	GLU343

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00558

Chain	Residue	Details
A	SER3
B	SER3

---

site_id	SWS_FT_FI7
Number of Residues	20
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P00558

Chain	Residue	Details
A	LYS10
A	LYS290
B	LYS10
B	LYS47
B	LYS74
B	LYS85
B	LYS96
B	LYS130
B	LYS145
B	LYS198
B	LYS266
A	LYS47
B	LYS290
A	LYS74
A	LYS85
A	LYS96
A	LYS130
A	LYS145
A	LYS198
A	LYS266

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P00558

Chain	Residue	Details
A	TYR195
B	TYR195

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 13pk

Chain	Residue	Details
A	ARG38
A	LYS215
A	GLY396

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

Chain	Residue	Details
B	ARG38
B	LYS215
B	GLY396

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