1LRK

Crystal Structure of Escherichia coli UDP-Galactose 4-Epimerase Mutant Y299C Complexed with UDP-N-acetylglucosamine

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003978	molecular_function	UDP-glucose 4-epimerase activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005975	biological_process	carbohydrate metabolic process
A	0005996	biological_process	monosaccharide metabolic process
A	0006012	biological_process	galactose metabolic process
A	0009242	biological_process	colanic acid biosynthetic process
A	0016853	molecular_function	isomerase activity
A	0016857	molecular_function	racemase and epimerase activity, acting on carbohydrates and derivatives
A	0033499	biological_process	galactose catabolic process via UDP-galactose, Leloir pathway
A	0042802	molecular_function	identical protein binding
A	0070403	molecular_function	NAD+ binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA A 342

Chain	Residue
A	GLN91
A	HOH437
A	HOH438
A	HOH484
A	HOH588
A	HOH676

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA A 343

Chain	Residue
A	HOH559
A	HOH878
A	GLN334
A	HOH388
A	HOH558

---

site_id	AC3
Number of Residues	31
Details	BINDING SITE FOR RESIDUE NAD A 340

Chain	Residue
A	GLY7
A	GLY10
A	TYR11
A	ILE12
A	ASP31
A	ASN32
A	LEU33
A	CYS34
A	ASN35
A	SER36
A	GLY57
A	ASP58
A	ILE59
A	PHE80
A	ALA81
A	GLY82
A	LYS84
A	ASN99
A	SER123
A	SER124
A	TYR149
A	LYS153
A	TYR177
A	PHE178
A	HOH349
A	HOH350
A	HOH380
A	HOH430
A	HOH431
A	HOH678
A	HOH704

---

site_id	AC4
Number of Residues	23
Details	BINDING SITE FOR RESIDUE UD1 A 341

Chain	Residue
A	VAL86
A	THR126
A	ASN179
A	ASN198
A	ASN199
A	LEU200
A	LEU215
A	ALA216
A	ILE217
A	PHE218
A	GLY229
A	ARG231
A	TYR233
A	VAL269
A	ARG292
A	ASP295
A	HOH455
A	HOH628
A	HOH670
A	HOH673
A	HOH679
A	HOH688
A	HOH702

---

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PGE A 344

Chain	Residue
A	LEU250
A	LYS253
A	TYR259

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"8611497","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12019271","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1579570","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8611497","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8611559","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8931134","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9174344","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9271498","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9271499","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9708982","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	11
Details	Binding site: {}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
A	TYR149
A	SER124
A	LYS153

---

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
A	ASN100
A	THR126
A	TYR149
A	LYS153

---

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
A	GLN146
A	LYS153

---

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
A	TYR149
A	LYS153

---

site_id	MCSA1
Number of Residues	3
Details	M-CSA 188

Chain	Residue	Details
A	SER124	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
A	TYR149	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	LYS153	activator, hydrogen bond donor

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