Structure of PDB 1x87 Chain B

Receptor sequence
>1x87B (length=493) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence]
AGTERRAKGWIQEAALRMLNNNLHPDVAERPDELKAARNWECYEAIVDTL
LRLENDETLLIQSGKPVAVFRTHPDAPRVLIANSNAGSWIYIGSQGIVQG
TYETFAEVARQHFGGTLAGTITLTAGLGGMGGAQPLAVTMNGGVCLAIEV
DPARIQRRIDTNYLDTMTDSLDAALEMAKQAKEEKKALSIGLVGNAAEVL
PRLVETGFVPDVLTDQTSAHDPLNGYIPAGLTLDEAAELRARDPKQYIAR
AKQSIAAHVRAMLAMQKQGAVTFDYGNNIRQVAKDEGVDDAFSFPGFVPA
YIRPLFCEGKGPFRWVALSGDPEDIYKTDEVILREFSDNERLCHWIRMAQ
KRIKFQGLPARICWLGYGERAKFGKIINDMVAKGELKAPIVIGRDEGMKD
GSDAIADWPILNALLNAVGGASWVSVHHGGGVGMGYSIHAGMVIVADGTK
EAEKRLERVLTTDPGLGVIRHADAGYELAIRTAKEKGIDMPML
3D structure
PDB1x87 2.4A X-ray structure of Urocanase protein complexed with NAD
ChainB
Resolution2.4 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.2.1.49: urocanate hydratase.
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 B G169 G171 G172 M173 E192 V193 R197 N238 A239 Q259 T260 H263 Y269 I270 Y318 N320 F340 G126 G128 G129 M130 E149 V150 R154 N195 A196 Q216 T217 H220 Y226 I227 Y275 N277 F297
Gene Ontology
Molecular Function
GO:0016153 urocanate hydratase activity
GO:0016829 lyase activity
Biological Process
GO:0006547 L-histidine metabolic process
GO:0006548 L-histidine catabolic process
GO:0019556 L-histidine catabolic process to glutamate and formamide
GO:0019557 L-histidine catabolic process to glutamate and formate
Cellular Component
GO:0005737 cytoplasm

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Cellular Component
External links
PDB RCSB:1x87, PDBe:1x87, PDBj:1x87
PDBsum1x87
PubMed
UniProtQ5L084|HUTU_GEOKA Urocanate hydratase (Gene Name=hutU)

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