Structure of PDB 2his Chain A

Receptor sequence
>2hisA (length=312) Species: 1708 (Cellulomonas fimi) [Search protein sequence]
ATTLKEAADGAGRDFGFALDPNRLSEAQYKAIADSEFNLVVAENAMKWDA
TEPSQNSFSFGAGDRVASYAADTGKELYGHTLVWHSQLPDWAKNLNGSAF
ESAMVNHVTKVADHFEGKVASWDVVNAAFADGGGRRQDSAFQQKLGNGYI
ETAFRAARAADPTAKLCINDYNVEGINAKSNSLYDLVKDFKARGVPLDCV
GFQSNLIVGQVPGDFRQNLQRFADLGVDVRITELDIRMRTPSDATKLATQ
AADYKKVVQACMQVTRCQGVTVWGITDKYSWVPDVFPGEGAALVWDASYA
KKPAYAAVMEAF
3D structure
PDB2his Insights into transition state stabilization of the beta-1,4-glycosidase Cex by covalent intermediate accumulation in active site mutants.
ChainA
Resolution1.84 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A127 N169 N205 E233 D235
Catalytic site (residue number reindexed from 1) A127 N169 N205 E233 D235
Enzyme Commision number 3.2.1.8: endo-1,4-beta-xylanase.
3.2.1.91: cellulose 1,4-beta-cellobiosidase (non-reducing end).
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 GLC A K47 H80 Q203 E233 W273 W281 K47 H80 Q203 E233 W273 W281
BS02 BGC A E43 N44 E43 N44
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2his, PDBe:2his, PDBj:2his
PDBsum2his
PubMed9731776
UniProtP07986|GUX_CELFI Exoglucanase/xylanase (Gene Name=cex)

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