4HN0

Crystal Structure of ChmJ, a 3'-monoepimerase apoenzyme from Streptomyces bikiniensis

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000271	biological_process	polysaccharide biosynthetic process
A	0005829	cellular_component	cytosol
A	0008830	molecular_function	dTDP-4-dehydrorhamnose 3,5-epimerase activity
A	0016853	molecular_function	isomerase activity
A	0016854	molecular_function	racemase and epimerase activity
A	0017000	biological_process	antibiotic biosynthetic process
A	0019305	biological_process	dTDP-rhamnose biosynthetic process
B	0000271	biological_process	polysaccharide biosynthetic process
B	0005829	cellular_component	cytosol
B	0008830	molecular_function	dTDP-4-dehydrorhamnose 3,5-epimerase activity
B	0016853	molecular_function	isomerase activity
B	0016854	molecular_function	racemase and epimerase activity
B	0017000	biological_process	antibiotic biosynthetic process
B	0019305	biological_process	dTDP-rhamnose biosynthetic process
C	0000271	biological_process	polysaccharide biosynthetic process
C	0005829	cellular_component	cytosol
C	0008830	molecular_function	dTDP-4-dehydrorhamnose 3,5-epimerase activity
C	0016853	molecular_function	isomerase activity
C	0016854	molecular_function	racemase and epimerase activity
C	0017000	biological_process	antibiotic biosynthetic process
C	0019305	biological_process	dTDP-rhamnose biosynthetic process
D	0000271	biological_process	polysaccharide biosynthetic process
D	0005829	cellular_component	cytosol
D	0008830	molecular_function	dTDP-4-dehydrorhamnose 3,5-epimerase activity
D	0016853	molecular_function	isomerase activity
D	0016854	molecular_function	racemase and epimerase activity
D	0017000	biological_process	antibiotic biosynthetic process
D	0019305	biological_process	dTDP-rhamnose biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 201

Chain	Residue
A	HIS17
A	ASP19
A	ARG21
A	GLY22
A	SER24
B	ARG57

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 202

Chain	Residue
A	TYR71
A	HOH333
A	PHE28
A	ARG29
A	SER32

---

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO A 203

Chain	Residue
A	ASN47
A	LYS70
A	TYR130

---

site_id	AC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE EDO A 204

Chain	Residue
A	ARG95

---

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL A 205

Chain	Residue
A	ARG57
B	ARG21

---

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO B 201

Chain	Residue
A	ARG57
B	HIS17
B	ASP19
B	ARG21
B	GLY22
B	SER24

---

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO B 202

Chain	Residue
B	GLN12
B	PHE28
B	ARG29
B	SER32
B	TYR71
B	HOH329

---

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO B 203

Chain	Residue
B	ASN47
B	LYS70
B	TYR130

---

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO B 204

Chain	Residue
B	SER5
B	GLU7
B	HOH331

---

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO B 205

Chain	Residue
B	MET1
B	TRP10
B	ALA36

---

site_id	BC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL B 206

Chain	Residue
A	ARG21
B	ARG57

---

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO C 201

Chain	Residue
C	HIS17
C	ASP19
C	ARG21
C	GLY22
C	SER24
D	ARG57

---

site_id	BC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL C 202

Chain	Residue
C	ARG57
C	HIS60
D	ARG21

---

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL C 203

Chain	Residue
C	ARG21
D	ARG57
D	HIS60

---

site_id	BC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO D 201

Chain	Residue
C	ARG57
D	HIS17
D	ASP19
D	ARG21
D	GLY22
D	ARG23
D	SER24

---

site_id	BC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO D 202

Chain	Residue
D	GLN12
D	PHE28
D	ARG29
D	TYR71

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"23116432","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"23116432","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"23116432","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4HN1","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"23116432","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4HMZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4HN1","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9HU21","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	Site: {"description":"Participates in a stacking interaction with the thymidine ring of dTDP-4-oxo-6-deoxyglucose","evidences":[{"source":"PubMed","id":"23116432","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4HN1","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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