1BOT

CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN ESCHERICHIA COLI GLYCEROL KINASE AND THE ALLOSTERIC REGULATOR FRUCTOSE 1,6-BISPHOSPHATE.

Functional Information from GO Data

Chain	GOid	namespace	contents
O	0000166	molecular_function	nucleotide binding
O	0003824	molecular_function	catalytic activity
O	0004370	molecular_function	glycerol kinase activity
O	0005515	molecular_function	protein binding
O	0005524	molecular_function	ATP binding
O	0005829	cellular_component	cytosol
O	0005975	biological_process	carbohydrate metabolic process
O	0006071	biological_process	glycerol metabolic process
O	0006072	biological_process	glycerol-3-phosphate metabolic process
O	0006974	biological_process	DNA damage response
O	0008270	molecular_function	zinc ion binding
O	0016301	molecular_function	kinase activity
O	0016740	molecular_function	transferase activity
O	0016773	molecular_function	phosphotransferase activity, alcohol group as acceptor
O	0019563	biological_process	glycerol catabolic process
O	0042802	molecular_function	identical protein binding
O	0046872	molecular_function	metal ion binding
Z	0000166	molecular_function	nucleotide binding
Z	0003824	molecular_function	catalytic activity
Z	0004370	molecular_function	glycerol kinase activity
Z	0005515	molecular_function	protein binding
Z	0005524	molecular_function	ATP binding
Z	0005829	cellular_component	cytosol
Z	0005975	biological_process	carbohydrate metabolic process
Z	0006071	biological_process	glycerol metabolic process
Z	0006072	biological_process	glycerol-3-phosphate metabolic process
Z	0006974	biological_process	DNA damage response
Z	0008270	molecular_function	zinc ion binding
Z	0016301	molecular_function	kinase activity
Z	0016740	molecular_function	transferase activity
Z	0016773	molecular_function	phosphotransferase activity, alcohol group as acceptor
Z	0019563	biological_process	glycerol catabolic process
Z	0042802	molecular_function	identical protein binding
Z	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE EPE O 602

Chain	Residue
O	HIS179
O	ASP198
O	TRP199
O	ARG211
O	GLU212
O	LEU214
O	PRO215
O	GLU216
O	VAL217

---

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL O 601

Chain	Residue
O	ARG83
O	GLU84
O	TRP103
O	TYR135
O	ASP245
O	GLN246
O	PHE270

---

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL Z 603

Chain	Residue
Z	ARG83
Z	GLU84
Z	TRP103
Z	TYR135
Z	ASP245
Z	GLN246
Z	PHE270

---

Functional Information from PROSITE/UniProt

site_id	PS00445
Number of Residues	21
Details	FGGY_KINASES_2 FGGY family of carbohydrate kinases signature 2. GaIFGLtrgvnan.HIIRATLE

Chain	Residue	Details
O	GLY362-GLU382

---

site_id	PS00933
Number of Residues	13
Details	FGGY_KINASES_1 FGGY family of carbohydrate kinases signature 1. YfSgtKVKWILDH

Chain	Residue	Details
O	TYR135-HIS147

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8170944","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1GLC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GLD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GLE","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10090737","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1BWF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GLJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GLL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10090737","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1GLJ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8170944","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8430315","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9817843","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1GLB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GLD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GLE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GLF","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9843423","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BO5","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8430315","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9843423","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BO5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1BOT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10090737","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1BWF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GLL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8170944","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8430315","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1GLB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GLC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GLD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GLE","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	Modified residue: {"description":"N6-malonyllysine","evidences":[{"source":"PubMed","id":"21908771","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---