1PM7

RmlC (dTDP-6-DEOXY-D-XYLO-4-HEXULOSE 3,5-EPIMERASE)STRUCTURE FROM MYCOBACTERIUM TUBERCULOSIS AND INHIBITOR DESIGN. THE APO STRUCTURE.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005829	cellular_component	cytosol
A	0008830	molecular_function	dTDP-4-dehydrorhamnose 3,5-epimerase activity
A	0016853	molecular_function	isomerase activity
A	0019305	biological_process	dTDP-rhamnose biosynthetic process
A	0045226	biological_process	extracellular polysaccharide biosynthetic process
B	0005515	molecular_function	protein binding
B	0005829	cellular_component	cytosol
B	0008830	molecular_function	dTDP-4-dehydrorhamnose 3,5-epimerase activity
B	0016853	molecular_function	isomerase activity
B	0019305	biological_process	dTDP-rhamnose biosynthetic process
B	0045226	biological_process	extracellular polysaccharide biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ACT A 260

Chain	Residue
A	HIS62
A	LYS72
A	HIS119

---

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ACT B 261

Chain	Residue
B	HIS62
B	LYS72
B	HIS119

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 250

Chain	Residue
A	THR17
A	MET1
A	LYS2
A	PRO16

---

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL B 251

Chain	Residue
B	MET1
B	PRO16
B	GLU28
B	TRP29
B	LEU30
B	GLY34
B	PHE35
B	TYR73
B	HOH265
B	HOH309

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000305|PubMed:17046787, ECO:0007744|PDB:2IXC

Chain	Residue	Details
A	HIS62
B	HIS62

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q9HU21

Chain	Residue	Details
A	TYR132
B	TYR132

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:17046787, ECO:0007744|PDB:2IXC

Chain	Residue	Details
A	ARG23
A	GLU28
A	ARG59
B	ARG23
B	GLU28
B	ARG59

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000305|PubMed:17046787, ECO:0007744|PDB:2IXC

Chain	Residue	Details
A	GLN47
B	GLN47

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:17046787, ECO:0000305|PubMed:12951098, ECO:0007744|PDB:1PM7

Chain	Residue	Details
A	LYS72
B	LYS72

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:17046787, ECO:0000305|PubMed:12951098, ECO:0007744|PDB:1PM7, ECO:0007744|PDB:2IXC

Chain	Residue	Details
A	HIS119
B	HIS119

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q9HU21

Chain	Residue	Details
A	GLU143
A	ARG170
B	GLU143
B	ARG170

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	SITE: Participates in a stacking interaction with the thymidine ring of dTDP-4-oxo-6-deoxyglucose => ECO:0000250|UniProtKB:Q5SFD1

Chain	Residue	Details
A	TYR138
B	TYR138

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1dzr

Chain	Residue	Details
A	HIS62
A	ASP171

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1dzr

Chain	Residue	Details
B	HIS62
B	ASP171

---