Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

13PK

TERNARY COMPLEX OF PHOSPHOGLYCERATE KINASE FROM TRYPANOSOMA BRUCEI

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	0005829	cellular_component	cytosol
A	0006094	biological_process	gluconeogenesis
A	0006096	biological_process	glycolytic process
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0020015	cellular_component	glycosome
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	0005829	cellular_component	cytosol
B	0006094	biological_process	gluconeogenesis
B	0006096	biological_process	glycolytic process
B	0016301	molecular_function	kinase activity
B	0016740	molecular_function	transferase activity
B	0020015	cellular_component	glycosome
B	0043531	molecular_function	ADP binding
B	0046872	molecular_function	metal ion binding
C	0000166	molecular_function	nucleotide binding
C	0004618	molecular_function	phosphoglycerate kinase activity
C	0005524	molecular_function	ATP binding
C	0005829	cellular_component	cytosol
C	0006094	biological_process	gluconeogenesis
C	0006096	biological_process	glycolytic process
C	0016301	molecular_function	kinase activity
C	0016740	molecular_function	transferase activity
C	0020015	cellular_component	glycosome
C	0043531	molecular_function	ADP binding
C	0046872	molecular_function	metal ion binding
D	0000166	molecular_function	nucleotide binding
D	0004618	molecular_function	phosphoglycerate kinase activity
D	0005524	molecular_function	ATP binding
D	0005829	cellular_component	cytosol
D	0006094	biological_process	gluconeogenesis
D	0006096	biological_process	glycolytic process
D	0016301	molecular_function	kinase activity
D	0016740	molecular_function	transferase activity
D	0020015	cellular_component	glycosome
D	0043531	molecular_function	ADP binding
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG A 422

Chain	Residue
A	ASP377
A	ADP421

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG B 422

Chain	Residue
B	ASP377
B	ADP421

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG C 422

Chain	Residue
C	ASP377
C	ADP421
C	PO4624

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG D 422

Chain	Residue
D	PO4625
D	ASP377
D	ADP421

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 C 624

Chain	Residue
C	ARG39
C	LYS219
C	GLY375
C	GLY376
C	GLY398
C	ADP421
C	MG422
C	HOH759

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 D 625

Chain	Residue
D	ARG39
D	LYS219
D	GLY375
D	GLY376
D	GLY398
D	ADP421
D	MG422
D	HOH747

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 A 701

Chain	Residue
A	LEU103
A	ARG105
D	PHE344
D	GLU345
D	LEU384

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 C 702

Chain	Residue
B	LYS48
B	LEU103
C	PHE354
C	LEU384
C	HOH789

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 C 703

Chain	Residue
B	PHE344
B	VAL347
B	LEU384
C	LEU103
C	ARG105

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 A 704

Chain	Residue
A	PHE344
A	VAL347
A	LEU384
A	HOH789
D	LYS48
D	LEU103

site_id	BC2
Number of Residues	23
Details	BINDING SITE FOR RESIDUE ADP A 421

Chain	Residue
A	GLY217
A	ALA218
A	LYS219
A	LYS223
A	GLY241
A	TYR245
A	ALA314
A	LEU315
A	ASN338
A	PRO340
A	GLY342
A	VAL343
A	GLU345
A	GLY374
A	GLY375
A	GLY376
A	ASP377
A	SER378
A	MG422
A	HOH716
A	HOH722
A	HOH842
A	HOH861

site_id	BC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE 3PG A 423

Chain	Residue
A	ASP24
A	ASN26
A	ARG39
A	HIS62
A	ARG65
A	ARG135
A	GLY168
A	ARG172
A	LYS219
A	HOH724
A	HOH752
A	HOH842
A	HOH876

site_id	BC4
Number of Residues	23
Details	BINDING SITE FOR RESIDUE ADP B 421

Chain	Residue
B	ASP377
B	SER378
B	MG422
B	HOH430
B	HOH442
B	HOH556
B	HOH579
B	GLY217
B	ALA218
B	LYS219
B	LYS223
B	GLY241
B	ALA242
B	TYR245
B	ALA314
B	LEU315
B	ASN338
B	PRO340
B	GLY342
B	VAL343
B	GLU345
B	GLY375
B	GLY376

site_id	BC5
Number of Residues	13
Details	BINDING SITE FOR RESIDUE 3PG B 423

Chain	Residue
B	ASP24
B	ASN26
B	ARG39
B	HIS62
B	GLY64
B	ARG65
B	ARG135
B	GLY168
B	ARG172
B	LYS219
B	GLY398
B	HOH480
B	HOH556

site_id	BC6
Number of Residues	19
Details	BINDING SITE FOR RESIDUE ADP C 421

Chain	Residue
C	GLY217
C	ALA218
C	LYS219
C	LYS223
C	GLY241
C	ALA242
C	TYR245
C	ALA314
C	ASN338
C	PRO340
C	GLY342
C	VAL343
C	GLU345
C	GLY375
C	GLY376
C	ASP377
C	SER378
C	MG422
C	PO4624

site_id	BC7
Number of Residues	21
Details	BINDING SITE FOR RESIDUE ADP D 421

Chain	Residue
D	GLY217
D	ALA218
D	LYS219
D	LYS223
D	GLY241
D	ALA242
D	TYR245
D	ALA314
D	ASN338
D	GLY339
D	PRO340
D	GLY342
D	VAL343
D	GLU345
D	GLY375
D	GLY376
D	ASP377
D	SER378
D	MG422
D	PO4625
D	HOH654

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LYS18-PRO28

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	44
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P00558","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9000079","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"13PK","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9000079","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9642090","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"13PK","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q7SIB7","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	a catalytic site defined by CSA, PubMed 9521762, 9384563

Chain	Residue	Details
A	GLY376
A	ARG39
A	LYS219
A	GLY399

site_id	CSA2
Number of Residues	4
Details	a catalytic site defined by CSA, PubMed 9521762, 9384563

Chain	Residue	Details
B	GLY376
B	ARG39
B	LYS219
B	GLY399

site_id	CSA3
Number of Residues	4
Details	a catalytic site defined by CSA, PubMed 9521762, 9384563

Chain	Residue	Details
C	GLY376
C	ARG39
C	LYS219
C	GLY399

site_id	CSA4
Number of Residues	4
Details	a catalytic site defined by CSA, PubMed 9521762, 9384563

Chain	Residue	Details
D	GLY376
D	ARG39
D	LYS219
D	GLY399

site_id	MCSA1
Number of Residues	4
Details	M-CSA 40

Chain	Residue	Details
A	ARG39	electrostatic stabiliser, hydrogen bond donor
A	LYS219	electrostatic stabiliser, hydrogen bond donor
A	GLY376	electrostatic stabiliser, hydrogen bond donor
A	GLY399	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA2
Number of Residues	4
Details	M-CSA 40

Chain	Residue	Details
B	ARG39	electrostatic stabiliser, hydrogen bond donor
B	LYS219	electrostatic stabiliser, hydrogen bond donor
B	GLY376	electrostatic stabiliser, hydrogen bond donor
B	GLY399	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA3
Number of Residues	4
Details	M-CSA 40

Chain	Residue	Details
C	ARG39	electrostatic stabiliser, hydrogen bond donor
C	LYS219	electrostatic stabiliser, hydrogen bond donor
C	GLY376	electrostatic stabiliser, hydrogen bond donor
C	GLY399	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA4
Number of Residues	4
Details	M-CSA 40

Chain	Residue	Details
D	ARG39	electrostatic stabiliser, hydrogen bond donor
D	LYS219	electrostatic stabiliser, hydrogen bond donor
D	GLY376	electrostatic stabiliser, hydrogen bond donor
D	GLY399	electrostatic stabiliser, hydrogen bond donor

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)