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PDBsum entry 4uqc

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protein ligands links
Hydrolase PDB id
4uqc

 

 

 

 

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Contents
Protein chain
390 a.a.
Ligands
TAR
TLA
GLC
Waters ×582
PDB id:
4uqc
Name: Hydrolase
Title: X-ray structure of glucuronoxylan-xylanohydrolase (xyn30a) from clostridium thermocellum at 1.30 a resolution
Structure: Carbohydrate binding family 6. Chain: a. Fragment: n-terminal catalytic module, residues 34-419. Synonym: xyn30a. Engineered: yes. Mutation: yes
Source: Ruminiclostridium thermocellum. Organism_taxid: 1515. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Resolution:
1.30Å     R-factor:   0.113     R-free:   0.141
Authors: F.Freire,A.K.Verma,A.Goyal,C.M.G.A.Fontes,S.Najmudin
Key ref: F.Freire et al. (2016). Conservation in the mechanism of glucuronoxylan hydrolysis revealed by the structure of glucuronoxylan xylanohydrolase (CtXyn30A) from Clostridium thermocellum. Acta Crystallogr D Struct Biol, 72, 1162-1173. PubMed id: 27841749 DOI: 10.1107/S2059798316014376
Date:
22-Jun-14     Release date:   24-Jun-15    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
A3DJS9  (A3DJS9_CLOTH) -  Carbohydrate binding family 6 from Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372)
Seq:
Struc:
 
Seq:
Struc:
630 a.a.
390 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 6 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.3.2.1.8  - endo-1,4-beta-xylanase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Endohydrolysis of 1,4-beta-D-xylosidic linkages in xylans.

 

 
DOI no: 10.1107/S2059798316014376 Acta Crystallogr D Struct Biol 72:1162-1173 (2016)
PubMed id: 27841749  
 
 
Conservation in the mechanism of glucuronoxylan hydrolysis revealed by the structure of glucuronoxylan xylanohydrolase (CtXyn30A) from Clostridium thermocellum.
F.Freire, A.Verma, P.Bule, V.D.Alves, C.M.Fontes, A.Goyal, S.Najmudin.
 
  ABSTRACT  
 
No abstract given.

 

 

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