1TZZ

Crystal structure of the protein L1841, unknown member of enolase superfamily from Bradyrhizobium japonicum

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0003824	molecular_function	catalytic activity
A	0016829	molecular_function	lyase activity
A	0016836	molecular_function	hydro-lyase activity
A	0034194	biological_process	D-galactonate catabolic process
A	0046872	molecular_function	metal ion binding
A	0047808	molecular_function	D(-)-tartrate dehydratase activity
A	0051260	biological_process	protein homooligomerization
B	0000287	molecular_function	magnesium ion binding
B	0003824	molecular_function	catalytic activity
B	0016829	molecular_function	lyase activity
B	0016836	molecular_function	hydro-lyase activity
B	0034194	biological_process	D-galactonate catabolic process
B	0046872	molecular_function	metal ion binding
B	0047808	molecular_function	D(-)-tartrate dehydratase activity
B	0051260	biological_process	protein homooligomerization

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 3501

Chain	Residue
A	ASP1216
A	GLU1242
A	GLU1268
A	HOH3322
A	HOH3323
A	HOH3324

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 3502

Chain	Residue
B	HOH3002
B	HOH3172
B	HOH3321
B	ASP2216
B	GLU2242
B	GLU2268

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"acceptor","evidences":[{"source":"PubMed","id":"17144653","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"17144653","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	26
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17144653","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	6
Details	Site: {"description":"Transition state stabilizer"}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Site: {"description":"Increases basicity of active site His"}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	5
Details	Annotated By Reference To The Literature 1ec9

Chain	Residue	Details
A	HIS1325
A	ASP1348
A	ASP1295
A	LYS1185
A	LYS1187

---

site_id	CSA2
Number of Residues	5
Details	Annotated By Reference To The Literature 1ec9

Chain	Residue	Details
B	LYS2185
B	LYS2187
B	ASP2295
B	HIS2325
B	ASP2348

---

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1ec9

Chain	Residue	Details
A	GLU1344
A	LYS1185
A	LYS1187

---

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1ec9

Chain	Residue	Details
B	LYS2185
B	LYS2187
B	GLU2344

---

site_id	MCSA1
Number of Residues	9
Details	M-CSA 463

Chain	Residue	Details
A	ASN1058	electrostatic stabiliser
A	LYS1185	electrostatic stabiliser
A	LYS1187	proton acceptor, proton donor
A	ASP1216	metal ligand
A	GLU1242	metal ligand
A	GLU1268	metal ligand
A	ASP1295	electrostatic stabiliser, increase basicity, modifies pKa
A	HIS1325	proton acceptor, proton donor
A	GLU1344	electrostatic stabiliser

---

site_id	MCSA2
Number of Residues	9
Details	M-CSA 463

Chain	Residue	Details
B	ASN2058	electrostatic stabiliser
B	LYS2185	electrostatic stabiliser
B	LYS2187	proton acceptor, proton donor
B	ASP2216	metal ligand
B	GLU2242	metal ligand
B	GLU2268	metal ligand
B	ASP2295	electrostatic stabiliser, increase basicity, modifies pKa
B	HIS2325	proton acceptor, proton donor
B	GLU2344	electrostatic stabiliser

---