1F6D

THE STRUCTURE OF UDP-N-ACETYLGLUCOSAMINE 2-EPIMERASE FROM E. COLI.

Functional Information from GO Data

Chain	GOid	namespace	contents
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	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	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	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	5
Details	BINDING SITE FOR RESIDUE NA A 1378

Chain	Residue
A	PRO298
A	SER350
A	ALA352
A	HOH1389
A	HOH1412

---

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL A 1379

Chain	Residue
A	HIS353
A	ASN354
A	HOH1384

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA B 2378

Chain	Residue
B	SER350
B	ALA352
B	HOH2402
B	HOH2487
B	PRO298

---

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL B 2379

Chain	Residue
B	GLY119
B	ARG121
B	ARG135

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA C 3378

Chain	Residue
C	PRO298
C	MSE349
C	SER350
C	ALA352

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL C 3379

Chain	Residue
C	GLY119
C	ARG121
C	ARG135
C	HOH3388

---

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA D 4378

Chain	Residue
D	PRO298
D	GLY301
D	SER350
D	ALA352
D	HOH4386
D	HOH4418

---

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL D 4379

Chain	Residue
D	ASN354
D	HOH4383

---

site_id	AC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE UDP A 1377

Chain	Residue
A	ARG10
A	ILE14
A	GLN271
A	TYR273
A	PHE276
A	GLY292
A	GLU296
A	HOH1567

---

site_id	BC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE UDP B 2377

Chain	Residue
B	ARG10
B	PRO11
B	ILE14
B	HIS213
B	GLN271
B	TYR273
B	PHE276
B	SER290
B	GLY291
B	GLY292
B	GLU296
B	HOH2385
B	HOH2435
B	HOH2455
B	HOH2483
B	HOH2532

---

site_id	BC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE UDP C 3377

Chain	Residue
C	ARG10
C	PRO11
C	ILE14
C	HIS213
C	GLN271
C	TYR273
C	PHE276
C	SER290
C	GLY291
C	GLY292
C	GLU296
C	HOH3387
C	HOH3497

---

site_id	BC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE UDP D 4377

Chain	Residue
D	ARG10
D	ILE14
D	GLN271
D	TYR273
D	PHE276
D	GLY292
D	GLU296

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02028, ECO:0000269|PubMed:11106477, ECO:0000269|PubMed:16021622

Chain	Residue	Details
A	ARG10
B	PHE276
B	SER290
B	GLU296
C	ARG10
C	HIS213
C	GLN271
C	PHE276
C	SER290
C	GLU296
D	ARG10
A	HIS213
D	HIS213
D	GLN271
D	PHE276
D	SER290
D	GLU296
A	GLN271
A	PHE276
A	SER290
A	GLU296
B	ARG10
B	HIS213
B	GLN271

---

site_id	SWS_FT_FI2
Number of Residues	16
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02028, ECO:0000269|PubMed:16021622

Chain	Residue	Details
A	LYS15
C	ASP95
C	GLU117
C	ARG313
D	LYS15
D	ASP95
D	GLU117
D	ARG313
A	ASP95
A	GLU117
A	ARG313
B	LYS15
B	ASP95
B	GLU117
B	ARG313
C	LYS15

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	6
Details	a catalytic site defined by CSA, PubMed 1110647, 18188181, 15518580

Chain	Residue	Details
A	HIS213
A	ARG215
A	ASP95
A	GLU117
A	GLU131
A	HIS246

---

site_id	MCSA1
Number of Residues	6
Details	M-CSA 544

Chain	Residue	Details
A	ASP95	electrostatic stabiliser, proton acceptor
A	GLU117	electrostatic stabiliser, proton shuttle (general acid/base)
A	GLU131	electrostatic stabiliser, proton shuttle (general acid/base)
A	HIS213	proton shuttle (general acid/base)
A	ARG215	electrostatic stabiliser
A	HIS246	electrostatic stabiliser

---

site_id	MCSA2
Number of Residues	6
Details	M-CSA 544

Chain	Residue	Details
B	ASP95	electrostatic stabiliser, proton acceptor
B	GLU117	electrostatic stabiliser, proton shuttle (general acid/base)
B	GLU131	electrostatic stabiliser, proton shuttle (general acid/base)
B	HIS213	proton shuttle (general acid/base)
B	ARG215	electrostatic stabiliser
B	HIS246	electrostatic stabiliser

---

site_id	MCSA3
Number of Residues	6
Details	M-CSA 544

Chain	Residue	Details
C	ASP95	electrostatic stabiliser, proton acceptor
C	GLU117	electrostatic stabiliser, proton shuttle (general acid/base)
C	GLU131	electrostatic stabiliser, proton shuttle (general acid/base)
C	HIS213	proton shuttle (general acid/base)
C	ARG215	electrostatic stabiliser
C	HIS246	electrostatic stabiliser

---

site_id	MCSA4
Number of Residues	6
Details	M-CSA 544

Chain	Residue	Details
D	ASP95	electrostatic stabiliser, proton acceptor
D	GLU117	electrostatic stabiliser, proton shuttle (general acid/base)
D	GLU131	electrostatic stabiliser, proton shuttle (general acid/base)
D	HIS213	proton shuttle (general acid/base)
D	ARG215	electrostatic stabiliser
D	HIS246	electrostatic stabiliser

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