1LVH

The Structure of Phosphorylated beta-phosphoglucomutase from Lactoccocus lactis to 2.3 angstrom resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0005737	cellular_component	cytoplasm
A	0005975	biological_process	carbohydrate metabolic process
A	0008801	molecular_function	beta-phosphoglucomutase activity
A	0016853	molecular_function	isomerase activity
A	0046872	molecular_function	metal ion binding
B	0000287	molecular_function	magnesium ion binding
B	0005737	cellular_component	cytoplasm
B	0005975	biological_process	carbohydrate metabolic process
B	0008801	molecular_function	beta-phosphoglucomutase activity
B	0016853	molecular_function	isomerase activity
B	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG B 800

Chain	Residue
B	PHD8
B	ASP10
B	GLU169
B	ASP170

---

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A 801

Chain	Residue
A	PHD8
A	ASP10
A	ASP170

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"15996095","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19154134","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"15996095","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19154134","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12081483","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12637673","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15826149","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15996095","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20164409","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LVH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O03","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O08","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Z4N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Z4O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ZOL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WF5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WF6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WHE","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20164409","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12637673","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1O03","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O08","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WF5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WF6","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20164409","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12637673","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15826149","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1O03","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O08","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Z4N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Z4O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WF5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WF6","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	Site: {"description":"Important for catalytic activity and assists the phosphoryl transfer reaction to Asp8 by balancing charge and orienting the reacting groups"}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"4-aspartylphosphate","evidences":[{"source":"PubMed","id":"15996095","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19154134","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details

Chain	Residue	Details
A	LYS145
A	PHD8
A	SER114

---

site_id	CSA2
Number of Residues	2
Details

Chain	Residue	Details
B	LYS145
B	SER114

---

site_id	MCSA1
Number of Residues	10
Details	M-CSA 206

Chain	Residue	Details
A	PHD8	metal ligand, nucleofuge, nucleophile
A	GLY174	metal ligand
A	ILE13	electrostatic stabiliser, hydrogen bond donor
A	THR14	metal ligand, proton acceptor, proton donor
A	HIS20	electrostatic stabiliser
A	ARG49	electrostatic stabiliser
A	ASN118	electrostatic stabiliser, hydrogen bond donor
A	GLY119	electrostatic stabiliser, hydrogen bond donor
A	ASP149	electrostatic stabiliser, hydrogen bond donor
A	ALA173	metal ligand

---

site_id	MCSA2
Number of Residues	10
Details	M-CSA 206

Chain	Residue	Details
B	PHD8	metal ligand, nucleofuge, nucleophile
B	GLY174	metal ligand
B	ILE13	electrostatic stabiliser, hydrogen bond donor
B	THR14	metal ligand, proton acceptor, proton donor
B	HIS20	electrostatic stabiliser
B	ARG49	electrostatic stabiliser
B	ASN118	electrostatic stabiliser, hydrogen bond donor
B	GLY119	electrostatic stabiliser, hydrogen bond donor
B	ASP149	electrostatic stabiliser, hydrogen bond donor
B	ALA173	metal ligand

---