Structure of PDB 4doe Chain A

Receptor sequence
>4doeA (length=454) Species: 31899 (Caldicellulosiruptor bescii) [Search protein sequence]
ASGSFNYGEALQKAIMFYEFQMSGKLPNWVRNNWRGDSALKDGQDNGLDL
TGGWFDAGDHVKFNLPMSYTGTMLSWAVYEYKDAFVKSGQLEHILNQIEW
VNDYFVKCHPSKYVYYYQVGDGSKDHAWWGPAEVMQMERPSFKVTQSSPG
STVVAETAASLAAASIVLKDRNPTKAATYLQHAKELYEFAEVTKSDAGYT
AANGYYNSWSGFYDELSWAAVWLYLATNDSTYLTKAESYVQNWPKISGSN
TIDYKWAHCWDDVHNGAALLLAKITGKDIYKQIIESHLDYWTTGYNGERI
KYTPKGLAWLDQWGSLRYATTTAFLAFVYSDWVGCPSTKKEIYRKFGESQ
IDYALGSAGRSFVVGFGTNPPKRPHHRTAHSSWADSQSIPSYHRHTLYGA
LVGGPGSDDSYTDDISNYVNNEVACDYNAGFVGALAKMYQLYGGNPIPDF
KAIE
3D structure
PDB4doe Revealing nature's cellulase diversity: the digestion mechanism of Caldicellulosiruptor bescii CelA.
ChainA
Resolution1.561 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D77 D80 Y227 E443
Catalytic site (residue number reindexed from 1) D56 D59 Y206 E422
Enzyme Commision number 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 H396 R398 Y439 E443 H375 R377 Y418 E422
BS02 BGC A W281 W334 R338 W260 W313 R317
BS03 BGC A W277 C280 W281 Y339 W256 C259 W260 Y318
BS04 BGC A W277 D282 D283 W256 D261 D262
BS05 CA A S231 G232 D235 E236 D282 S210 G211 D214 E215 D261
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:4doe, PDBe:4doe, PDBj:4doe
PDBsum4doe
PubMed24357319
UniProtP96311

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