5JQX

Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with phosphoglyceric acid (PGA) - GpgS*PGA

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0006011	biological_process	UDP-glucose metabolic process
A	0016757	molecular_function	glycosyltransferase activity
A	0016758	molecular_function	hexosyltransferase activity
A	0042803	molecular_function	protein homodimerization activity
A	0046872	molecular_function	metal ion binding
B	0000287	molecular_function	magnesium ion binding
B	0006011	biological_process	UDP-glucose metabolic process
B	0016757	molecular_function	glycosyltransferase activity
B	0016758	molecular_function	hexosyltransferase activity
B	0042803	molecular_function	protein homodimerization activity
B	0046872	molecular_function	metal ion binding
C	0000287	molecular_function	magnesium ion binding
C	0006011	biological_process	UDP-glucose metabolic process
C	0016757	molecular_function	glycosyltransferase activity
C	0016758	molecular_function	hexosyltransferase activity
C	0042803	molecular_function	protein homodimerization activity
C	0046872	molecular_function	metal ion binding
D	0000287	molecular_function	magnesium ion binding
D	0006011	biological_process	UDP-glucose metabolic process
D	0016757	molecular_function	glycosyltransferase activity
D	0016758	molecular_function	hexosyltransferase activity
D	0042803	molecular_function	protein homodimerization activity
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	binding site for residue 3PG A 401

Chain	Residue
A	GLY182
A	HOH507
A	HOH514
A	GLY183
A	GLY184
A	ARG185
A	VAL186
A	THR187
A	HIS258
A	MET269
A	HOH505

---

site_id	AC2
Number of Residues	8
Details	binding site for residue 3PG B 401

Chain	Residue
B	GLY183
B	GLY184
B	ARG185
B	VAL186
B	THR187
B	HIS258
B	ASN260
B	MET269

---

site_id	AC3
Number of Residues	9
Details	binding site for residue 3PG C 401

Chain	Residue
C	GLY183
C	GLY184
C	ARG185
C	VAL186
C	THR187
C	HIS258
C	ASN260
C	MET269
C	HOH516

---

site_id	AC4
Number of Residues	8
Details	binding site for residue 3PG D 401

Chain	Residue
D	GLY182
D	GLY183
D	GLY184
D	ARG185
D	VAL186
D	THR187
D	HIS258
D	MET269

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	28
Details	BINDING: BINDING => ECO:0000269|PubMed:26136334, ECO:0007744|PDB:4Y6N, ECO:0007744|PDB:4Y6U, ECO:0007744|PDB:4Y7F, ECO:0007744|PDB:4Y7G, ECO:0007744|PDB:4Y9X

Chain	Residue	Details
A	PRO50
B	LYS114
B	ASP134
B	ASP136
B	TYR229
B	HIS258
C	PRO50
C	SER81
C	LYS114
C	ASP134
C	ASP136
A	SER81
C	TYR229
C	HIS258
D	PRO50
D	SER81
D	LYS114
D	ASP134
D	ASP136
D	TYR229
D	HIS258
A	LYS114
A	ASP134
A	ASP136
A	TYR229
A	HIS258
B	PRO50
B	SER81

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:26136334, ECO:0000269|PubMed:28625787, ECO:0007744|PDB:4Y6N, ECO:0007744|PDB:4Y6U, ECO:0007744|PDB:4Y9X, ECO:0007744|PDB:5JQX

Chain	Residue	Details
A	GLY184
B	GLY184
C	GLY184
D	GLY184

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:28625787, ECO:0007744|PDB:5JT0

Chain	Residue	Details
A	ARG256
B	ARG256
C	ARG256
D	ARG256

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:26136334, ECO:0007744|PDB:4Y6N, ECO:0007744|PDB:4Y6U

Chain	Residue	Details
A	ASN260
B	ASN260
C	ASN260
D	ASN260

---