Structure of PDB 1ia7 Chain A Binding Site BS03

Receptor Information

>1ia7 Chain A (length=431) Species: 1521 (Ruminiclostridium cellulolyticum)

AGTHDYSTALKDSIIFFDANKCGPQAGENNVFDWRGACHTTDGSDVGVDL
TGGYHDAGDHVKFGLPQGYSAAILGWSLYEFKESFDATGNTTKMLQQLKY
FTDYFLKSHPNSTTFYYQVGEGNADHTYWGAPEEQTGQRPSLYKADPSSP
ASDILSETSAALTLMYLNYKNIDSAYATKCLNAAKELYAMGKANQGVGNG
QSFYQATSFGDDLAWAATWLYTATNDSTYITDAEQFITLGNTMNENKMQD
KWTMCWDDMYVPAALRLAQITGKQIYKDAIEFNFNYWKTQVTTTPGGLKW
LSNWGVLRYAAAESMVMLVYCKQNPDQSLLDLAKKQVDYILGDNPANMSY
IIGYGSNWCIHPHHRAANGYTYANGDNAKPAKHLLTGALVGGPDQNDKFL
DDANQYQYTEVALDYNAGLVGVLAGAIKFFG

Ligand information

• Ligand ID: CA
• InChI: InChI=1S/Ca/q+2
• InChIKey: BHPQYMZQTOCNFJ-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.341: [Ca++]
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Ca+2]
• Formula: Ca
• Name: CALCIUM ION
• DrugBank: DB14577
• PDB chain: 1ia7 Chain A Residue 1332

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1ia7 Crystal structure of the cellulase Cel9M enlightens structure/function relationships of the variable catalytic modules in glycoside hydrolases.
• Resolution: 2.0 Å
• Binding residue (original residue number in PDB): S208 D211 D212 D257
• Binding residue (residue number reindexed from 1): S208 D211 D212 D257
• Annotation score: 4

Enzymatic activity

• Catalytic site (original residue number in PDB): D56 D59 Y204 E410
• Catalytic site (residue number reindexed from 1): D56 D59 Y204 E410
• Enzyme Commision number: 3.2.1.-
  3.2.1.4: cellulase.

Gene Ontology

Molecular Function

• GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds

Biological Process

• GO:0005975 carbohydrate metabolic process

External links

• PDB: RCSB:1ia7, PDBe:1ia7, PDBj:1ia7
• PDBsum: 1ia7
• PubMed: 12220178
• UniProt: Q9EYQ2