9PZL

Pyruvate phosphate dikinase in complex with AMP-PNP and sulfate ions

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0005524	molecular_function	ATP binding
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0046872	molecular_function	metal ion binding
A	0050242	molecular_function	pyruvate, phosphate dikinase activity
B	0000166	molecular_function	nucleotide binding
B	0005524	molecular_function	ATP binding
B	0016301	molecular_function	kinase activity
B	0016740	molecular_function	transferase activity
B	0046872	molecular_function	metal ion binding
B	0050242	molecular_function	pyruvate, phosphate dikinase activity
C	0000166	molecular_function	nucleotide binding
C	0005524	molecular_function	ATP binding
C	0016301	molecular_function	kinase activity
C	0016740	molecular_function	transferase activity
C	0046872	molecular_function	metal ion binding
C	0050242	molecular_function	pyruvate, phosphate dikinase activity
D	0000166	molecular_function	nucleotide binding
D	0005524	molecular_function	ATP binding
D	0016301	molecular_function	kinase activity
D	0016740	molecular_function	transferase activity
D	0046872	molecular_function	metal ion binding
D	0050242	molecular_function	pyruvate, phosphate dikinase activity

Functional Information from PROSITE/UniProt

site_id	PS00370
Number of Residues	12
Details	PEP_ENZYMES_PHOS_SITE PEP-utilizing enzymes phosphorylation site signature. GGmTsHAAVVAR

Chain	Residue	Details
A	GLY450-ARG461

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site_id	PS00742
Number of Residues	19
Details	PEP_ENZYMES_2 PEP-utilizing enzymes signature 2. EfFSFGTNDLtQMTFGfsR

Chain	Residue	Details
A	GLU761-ARG779

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1352
Details	Region: {"description":"N-terminal"}

Chain

Residue

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site_id	SWS_FT_FI2
Number of Residues	236
Details	Region: {"description":"Linker 1"}

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Residue

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site_id	SWS_FT_FI3
Number of Residues	392
Details	Region: {"description":"Central"}

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Residue

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site_id	SWS_FT_FI4
Number of Residues	136
Details	Region: {"description":"Linker 2"}

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Residue

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site_id	SWS_FT_FI5
Number of Residues	4
Details	Active site: {"description":"Tele-phosphohistidine intermediate","evidences":[{"source":"PubMed","id":"11468288","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI6
Number of Residues	4
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"7857929","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"8610096","evidenceCode":"ECO:0000305"}]}

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Residue

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site_id	SWS_FT_FI7
Number of Residues	4
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}

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site_id	SWS_FT_FI8
Number of Residues	28
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8610096","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI9
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine; by PDRP1","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	9
Details	M-CSA 207

Chain	Residue	Details
A	LYS22	electrostatic stabiliser, hydrogen bond donor
A	ARG92	electrostatic stabiliser, hydrogen bond donor
A	GLY101	electrostatic stabiliser, hydrogen bond donor
A	MET103	electrostatic stabiliser, hydrogen bond donor
A	ARG337	electrostatic stabiliser, hydrogen bond donor
A	HIS455	covalently attached, nucleofuge, nucleophile, polar interaction
A	SER764	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
A	CYS831	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
A	TYR851	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay

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site_id	MCSA2
Number of Residues	9
Details	M-CSA 207

Chain	Residue	Details
B	LYS22	electrostatic stabiliser, hydrogen bond donor
B	ARG92	electrostatic stabiliser, hydrogen bond donor
B	GLY101	electrostatic stabiliser, hydrogen bond donor
B	MET103	electrostatic stabiliser, hydrogen bond donor
B	ARG337	electrostatic stabiliser, hydrogen bond donor
B	HIS455	covalently attached, nucleofuge, nucleophile, polar interaction
B	SER764	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
B	CYS831	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
B	TYR851	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay

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site_id	MCSA3
Number of Residues	9
Details	M-CSA 207

Chain	Residue	Details
C	LYS22	electrostatic stabiliser, hydrogen bond donor
C	ARG92	electrostatic stabiliser, hydrogen bond donor
C	GLY101	electrostatic stabiliser, hydrogen bond donor
C	MET103	electrostatic stabiliser, hydrogen bond donor
C	ARG337	electrostatic stabiliser, hydrogen bond donor
C	HIS455	covalently attached, nucleofuge, nucleophile, polar interaction
C	SER764	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
C	CYS831	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
C	TYR851	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay

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site_id	MCSA4
Number of Residues	9
Details	M-CSA 207

Chain	Residue	Details
D	LYS22	electrostatic stabiliser, hydrogen bond donor
D	ARG92	electrostatic stabiliser, hydrogen bond donor
D	GLY101	electrostatic stabiliser, hydrogen bond donor
D	MET103	electrostatic stabiliser, hydrogen bond donor
D	ARG337	electrostatic stabiliser, hydrogen bond donor
D	HIS455	covalently attached, nucleofuge, nucleophile, polar interaction
D	SER764	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
D	CYS831	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
D	TYR851	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay

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