Structure of PDB 2c20 Chain E

Receptor sequence
>2c20E (length=329) Species: 198094 (Bacillus anthracis str. Ames) [Search protein sequence]
NSILICGGAGYIGSHAVKKLVDEGLSVVVVDNLQTGHEDAITEGAKFYNG
DLRDKAFLRDVFTQENIEAVMHFAADSLVGVSMEKPLQYYNNNVYGALCL
LEVMDEFKVDKFIFSSTAATYGEVDVDLITEETMTNPTNTYGETKLAIEK
MLHWYSQASNLRYKIFRYFNVAGATPNGIIGEDHRPETHLIPLVLQVALG
QREKIMMFGDDYNTPDGTCIRDYIHVEDLVAAHFLGLKDLQNGGESDFYN
LGNGNGFSVKEIVDAVREVTNHEIPAEVAPRRAGDPARLVASSQKAKEKL
GWDPRYVNVKTIIEHAWNWHQKQPNGYEK
3D structure
PDB2c20 Crystal Structure of Udp-Glucose 4-Epimerase from Bacillus Anthracis at 2.7A Resolution
ChainE
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T118 A119 A120 Y142 K146 H185
Catalytic site (residue number reindexed from 1) T117 A118 A119 Y141 K145 H184
Enzyme Commision number 5.1.3.2: UDP-glucose 4-epimerase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 NAD E G8 G11 Y12 I13 D32 N33 T36 G37 D52 F74 A75 N93 Y142 K146 Y169 F170 V172 H185 G7 G10 Y11 I12 D31 N32 T35 G36 D51 F73 A74 N92 Y141 K145 Y168 F169 V171 H184
BS02 ZN E E183 H185 E188 H190 E182 H184 E187 H189
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003978 UDP-glucose 4-epimerase activity
GO:0016853 isomerase activity
GO:0046872 metal ion binding
Biological Process
GO:0006012 galactose metabolic process
GO:0033499 galactose catabolic process via UDP-galactose
Cellular Component
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:2c20, PDBe:2c20, PDBj:2c20
PDBsum2c20
PubMed
UniProtA0A6L8PTV5

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