1VGV

Crystal structure of UDP-N-acetylglucosamine_2 epimerase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000271	biological_process	polysaccharide biosynthetic process
A	0003824	molecular_function	catalytic activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0008761	molecular_function	UDP-N-acetylglucosamine 2-epimerase activity
A	0009246	biological_process	enterobacterial common antigen biosynthetic process
A	0016853	molecular_function	isomerase activity
A	0042803	molecular_function	protein homodimerization activity
B	0000271	biological_process	polysaccharide biosynthetic process
B	0003824	molecular_function	catalytic activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0008761	molecular_function	UDP-N-acetylglucosamine 2-epimerase activity
B	0009246	biological_process	enterobacterial common antigen biosynthetic process
B	0016853	molecular_function	isomerase activity
B	0042803	molecular_function	protein homodimerization activity
C	0000271	biological_process	polysaccharide biosynthetic process
C	0003824	molecular_function	catalytic activity
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0008761	molecular_function	UDP-N-acetylglucosamine 2-epimerase activity
C	0009246	biological_process	enterobacterial common antigen biosynthetic process
C	0016853	molecular_function	isomerase activity
C	0042803	molecular_function	protein homodimerization activity
D	0000271	biological_process	polysaccharide biosynthetic process
D	0003824	molecular_function	catalytic activity
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0008761	molecular_function	UDP-N-acetylglucosamine 2-epimerase activity
D	0009246	biological_process	enterobacterial common antigen biosynthetic process
D	0016853	molecular_function	isomerase activity
D	0042803	molecular_function	protein homodimerization activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	20
Details	BINDING SITE FOR RESIDUE UD1 B 385

Chain	Residue
B	ARG10
B	HIS213
B	GLN271
B	TYR273
B	PHE276
B	SER290
B	GLY291
B	GLY292
B	GLU296
B	ARG313
B	HOH439
B	PRO11
B	HOH453
B	GLU12
B	LYS15
B	HIS93
B	ASP95
B	THR96
B	GLU117
B	GLU131

---

site_id	AC2
Number of Residues	21
Details	BINDING SITE FOR RESIDUE UD1 C 385

Chain	Residue
C	THR9
C	ARG10
C	PRO11
C	GLU12
C	LYS15
C	HIS93
C	ASP95
C	GLU117
C	GLU131
C	ARG135
C	HIS213
C	GLN271
C	TYR273
C	PHE276
C	SER290
C	GLY291
C	GLY292
C	GLU296
C	ARG313
C	HOH427
C	HOH456

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	28
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02028","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11106477","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16021622","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02028","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16021622","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1f6d

Chain	Residue	Details
A	GLU131
A	ASP95
A	GLU117
A	HIS213

---

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1f6d

Chain	Residue	Details
B	GLU131
B	ASP95
B	GLU117
B	HIS213

---

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1f6d

Chain	Residue	Details
C	GLU131
C	ASP95
C	GLU117

---

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1f6d

Chain	Residue	Details
D	GLU131
D	ASP95
D	GLU117
D	HIS213

---

site_id	MCSA1
Number of Residues	6
Details	M-CSA 544

Chain	Residue	Details
A	ILE111	electrostatic stabiliser, proton acceptor
A	ALA133	electrostatic stabiliser, proton shuttle (general acid/base)
A	SER147	electrostatic stabiliser, proton shuttle (general acid/base)
A	ILE241	proton shuttle (general acid/base)
A	TYR243	electrostatic stabiliser
A	LEU274	electrostatic stabiliser

---

site_id	MCSA2
Number of Residues	6
Details	M-CSA 544

Chain	Residue	Details
B	ILE111	electrostatic stabiliser, proton acceptor
B	ALA133	electrostatic stabiliser, proton shuttle (general acid/base)
B	SER147	electrostatic stabiliser, proton shuttle (general acid/base)
B	ILE241	proton shuttle (general acid/base)
B	TYR243	electrostatic stabiliser
B	LEU274	electrostatic stabiliser

---

site_id	MCSA3
Number of Residues	6
Details	M-CSA 544

Chain	Residue	Details
C	ILE111	electrostatic stabiliser, proton acceptor
C	ALA133	electrostatic stabiliser, proton shuttle (general acid/base)
C	SER147	electrostatic stabiliser, proton shuttle (general acid/base)
C	ILE241	proton shuttle (general acid/base)
C	TYR243	electrostatic stabiliser
C	LEU274	electrostatic stabiliser

---

site_id	MCSA4
Number of Residues	6
Details	M-CSA 544

Chain	Residue	Details
D	ILE111	electrostatic stabiliser, proton acceptor
D	ALA133	electrostatic stabiliser, proton shuttle (general acid/base)
D	SER147	electrostatic stabiliser, proton shuttle (general acid/base)
D	ILE241	proton shuttle (general acid/base)
D	TYR243	electrostatic stabiliser
D	LEU274	electrostatic stabiliser

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