5OJZ

D10N variant of beta-phosphoglucomutase from Lactococcus lactis inhibited by a beryllium triflouride phosphoenzyme analogue to 1.3A 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

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue MG A 301

Chain	Residue
A	ASP8
A	ASN10
A	ASP170
A	BEF303
A	HOH432
A	HOH517

---

site_id	AC2
Number of Residues	6
Details	binding site for residue MG A 302

Chain	Residue
A	HOH638
A	HOH643
A	HOH644
A	HOH439
A	HOH585
A	HOH629

---

site_id	AC3
Number of Residues	10
Details	binding site for residue BEF A 303

Chain	Residue
A	ASP8
A	LEU9
A	ASN10
A	SER114
A	ALA115
A	LYS145
A	MG301
A	HOH432
A	HOH517
A	HOH588

---

site_id	AC4
Number of Residues	4
Details	binding site for residue EDO A 304

Chain	Residue
A	SER163
A	GLY182
A	LYS219
A	HOH491

---

site_id	AC5
Number of Residues	4
Details	binding site for residue EDO A 305

Chain	Residue
A	GLN54
A	HIS206
A	HOH452
A	HOH509

---

site_id	AC6
Number of Residues	4
Details	binding site for residue EDO A 306

Chain	Residue
A	PHE132
A	ASP133
A	HOH468
A	HOH485

---

site_id	AC7
Number of Residues	6
Details	binding site for residue EDO A 307

Chain	Residue
A	MET1
A	GLU140
A	TRP216
A	LEU217
A	GLN220
A	EDO308

---

site_id	AC8
Number of Residues	5
Details	binding site for residue EDO A 308

Chain	Residue
A	MET1
A	ASP137
A	TRP216
A	EDO307
A	HOH575

---

site_id	AC9
Number of Residues	4
Details	binding site for residue EDO A 309

Chain	Residue
A	GLU18
A	ARG38
A	LYS45
A	HOH421

---

site_id	AD1
Number of Residues	6
Details	binding site for residue EDO A 310

Chain	Residue
A	GLU29
A	ILE33
A	ASN34
A	GLY35
A	VAL36
A	HOH436

---

site_id	AD2
Number of Residues	6
Details	binding site for residue EDO A 311

Chain	Residue
A	ALA115
A	SER144
A	LYS145
A	HOH407
A	HOH423
A	HOH427

---

site_id	AD3
Number of Residues	6
Details	binding site for residue EDO A 312

Chain	Residue
A	TYR93
A	PRO94
A	ASP203
A	THR204
A	HOH401
A	HOH415

---

site_id	AD4
Number of Residues	6
Details	binding site for residue EDO A 313

Chain	Residue
A	ASP58
A	ASP61
A	SER88
A	PRO89
A	ALA90
A	HOH628

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
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	1
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	3
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	2
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	4
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	2
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	1
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	MCSA1
Number of Residues	10
Details	M-CSA 206

Chain	Residue	Details
A	ASP8	metal ligand, nucleofuge, nucleophile
A	ASP170	metal ligand
A	LEU9	electrostatic stabiliser, hydrogen bond donor
A	ASN10	metal ligand, proton acceptor, proton donor
A	THR16	electrostatic stabiliser
A	LYS45	electrostatic stabiliser
A	SER114	electrostatic stabiliser, hydrogen bond donor
A	ALA115	electrostatic stabiliser, hydrogen bond donor
A	LYS145	electrostatic stabiliser, hydrogen bond donor
A	GLU169	metal ligand

---