2E28

Crystal structure analysis of pyruvate kinase from Bacillus stearothermophilus

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0003824	molecular_function	catalytic activity
A	0004743	molecular_function	pyruvate kinase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0006096	biological_process	glycolytic process
A	0016301	molecular_function	kinase activity
A	0016310	biological_process	phosphorylation
A	0016772	molecular_function	transferase activity, transferring phosphorus-containing groups
A	0030955	molecular_function	potassium ion binding
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SO4 A 588

Chain	Residue
A	THR381
A	HOH692
A	VAL382
A	SER383
A	GLY384
A	LYS385
A	THR386
A	THR463
A	GLY464
A	HOH621

---

Functional Information from PROSITE/UniProt

site_id	PS00110
Number of Residues	13
Details	PYRUVATE_KINASE Pyruvate kinase active site signature. IqIIAKIENeEGV

Chain	Residue	Details
A	ILE216-VAL228

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	10
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P30613

Chain	Residue	Details
A	ARG33
A	THR279
A	ASN35
A	SER37
A	ASP67
A	THR68
A	LYS221
A	GLU223
A	GLY246
A	ASP247

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P14618

Chain	Residue	Details
A	ARG74
A	LYS157

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P00549, ECO:0000305|PubMed:15749828

Chain	Residue	Details
A	LYS221

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	6
Details	Annotated By Reference To The Literature 1pkn

Chain	Residue	Details
A	LYS221
A	SER313
A	GLU315
A	ARG74
A	ARG33
A	THR279

---