1PKN

STRUCTURE OF RABBIT MUSCLE PYRUVATE KINASE COMPLEXED WITH MN2+, K+, AND PYRUVATE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000287	molecular_function	magnesium ion binding
A	0003729	molecular_function	mRNA binding
A	0003824	molecular_function	catalytic activity
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0004713	molecular_function	protein tyrosine kinase activity
A	0004715	molecular_function	non-membrane spanning protein tyrosine kinase activity
A	0004743	molecular_function	pyruvate kinase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005791	cellular_component	rough endoplasmic reticulum
A	0006096	biological_process	glycolytic process
A	0006417	biological_process	regulation of translation
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0030955	molecular_function	potassium ion binding
A	0046872	molecular_function	metal ion binding
A	1903672	biological_process	positive regulation of sprouting angiogenesis
A	2000767	biological_process	positive regulation of cytoplasmic translation

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K A 532

Chain	Residue
A	ASN74
A	SER76
A	ASP112
A	THR113

---

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN A 534

Chain	Residue
A	GLU271
A	ASP295
A	PYR533

---

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PYR A 533

Chain	Residue
A	MET290
A	ALA292
A	GLY294
A	ASP295
A	THR327
A	MN534
A	LYS269
A	GLU271

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE264-VAL276

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	224
Details	Region: {"description":"Interaction with POU5F1","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	25
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P30613","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Site: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P00549","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	3
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P11980","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI13
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI14
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI15
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI16
Number of Residues	1
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI17
Number of Residues	3
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI18
Number of Residues	1
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI19
Number of Residues	2
Details	Modified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	6
Details	a catalytic site defined by CSA, PubMed 8193145

Chain	Residue	Details
A	LYS269
A	SER361
A	ARG119
A	GLU363
A	ARG72
A	THR327

---

site_id	MCSA1
Number of Residues	4
Details	M-CSA 326

Chain	Residue	Details
A	ARG72	attractive charge-charge interaction, electrostatic stabiliser, steric role
A	ARG119	attractive charge-charge interaction, electrostatic stabiliser, steric role
A	LYS269	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role
A	THR327	electrostatic stabiliser, hydrogen bond donor, increase acidity

---