Structure of PDB 4xeb Chain A

Receptor sequence
>4xebA (length=430) Species: 28572 (Talaromyces funiculosus) [Search protein sequence]
PQIGTYTAETHPSLSWSTCKSSCTTNSGAITLDANWRWVHGVNTSTNCYT
GNTWNSAICDTDASCAQDCALDGADYSGTYGITTSGNSLRLNFVTGSNVG
SRTYLMADNTHYQIFDLLNQEFTFTVDVSHLPCGLNGALYFVTMDADGGV
SKYPNNKAGAQYGVGYCDSQCPRDLKFIAGQANVEGWTPSANNANTGIGN
HGACCAELDIWEANSISEALTPHPCDTPGLSVCTTDACGGTYSSDRYAGT
CDPDGCDFNPYRLGVTDFYGSGKTVDTTKPFTVVTQFVTNDGTSTGSLSE
IRRYYVQNGVVIPQPSSKISGISGNVINSDYCAAEISTFGGTASFSKHGG
LTNMAAGMEAGMVLVMSLWDDYAVNMLWLDSTYPTNATGTPGAARGTCAT
TSGDPKTVESQSGSSYVTFSDIRVGPFNST
3D structure
PDB4xeb Engineering enhanced cellobiohydrolase activity
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E209 D211 E214 H225
Catalytic site (residue number reindexed from 1) E207 D209 E212 H223
Enzyme Commision number 3.2.1.-
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 BGC A R248 D256 R397 R246 D254 R395
BS02 BGC A H225 T243 R248 D256 W380 H223 T241 R246 D254 W378
BS03 BGC A R104 Y142 S369 W371 R102 Y140 S367 W369
BS04 BGC A W38 R104 D176 W36 R102 D174
BS05 BGC A N37 W38 V101 N35 W36 V99
BS06 BGC A W38 N100 K178 W36 N98 K176
BS07 BGC A W40 N49 W38 N47
BS08 BGC A W40 N49 W38 N47
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:4xeb, PDBe:4xeb, PDBj:4xeb
PDBsum4xeb
PubMed
UniProtF1CYZ0

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