Structure of PDB 1ia7 Chain A

Receptor sequence
>1ia7A (length=431) Species: 1521 (Ruminiclostridium cellulolyticum) [Search protein sequence]
AGTHDYSTALKDSIIFFDANKCGPQAGENNVFDWRGACHTTDGSDVGVDL
TGGYHDAGDHVKFGLPQGYSAAILGWSLYEFKESFDATGNTTKMLQQLKY
FTDYFLKSHPNSTTFYYQVGEGNADHTYWGAPEEQTGQRPSLYKADPSSP
ASDILSETSAALTLMYLNYKNIDSAYATKCLNAAKELYAMGKANQGVGNG
QSFYQATSFGDDLAWAATWLYTATNDSTYITDAEQFITLGNTMNENKMQD
KWTMCWDDMYVPAALRLAQITGKQIYKDAIEFNFNYWKTQVTTTPGGLKW
LSNWGVLRYAAAESMVMLVYCKQNPDQSLLDLAKKQVDYILGDNPANMSY
IIGYGSNWCIHPHHRAANGYTYANGDNAKPAKHLLTGALVGGPDQNDKFL
DDANQYQYTEVALDYNAGLVGVLAGAIKFFG
3D structure
PDB1ia7 Crystal structure of the cellulase Cel9M enlightens structure/function relationships of the variable catalytic modules in glycoside hydrolases.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 BGC A Y372 Y406 Y372 Y406
BS02 BGC A H126 H363 R365 Y406 E410 H126 H363 R365 Y406 E410
BS03 CA A S208 D211 D212 D257 S208 D211 D212 D257
BS04 ZN A C22 C38 H39 H55 C22 C38 H39 H55
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:1ia7, PDBe:1ia7, PDBj:1ia7
PDBsum1ia7
PubMed12220178
UniProtQ9EYQ2

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