Your browser does not support inline frames or is currently configured not to display inline frames. Content can be viewed at actual source page: inc/head.html
PDBsum entry 4mst
Go to PDB code:
Sugar binding protein
PDB id
4mst
Loading ...
Contents
Protein chains
241 a.a.
Metals
_CL
×2
Waters
×316
PDB id:
4mst
Links
PDBe
RCSB
MMDB
JenaLib
Proteopedia
CATH
SCOP
PDBSWS
PDBePISA
ProSAT
Name:
Sugar binding protein
Title:
Crystal structure of a putative catalytic domain of a chitinase-like protein (hbclp1) from hevea brasiliensis
Structure:
Class i chitinase. Chain: a, b. Fragment: putative catalytic domain (pcatd, unp residues 54-295). Synonym: chitinase-like lectin. Engineered: yes
Source:
Hevea brasiliensis. Para rubber tree. Organism_taxid: 3981. Strain: rimm600. Gene: hbchi-l1, rq30. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
1.93Å
R-factor:
0.168
R-free:
0.202
Authors:
S.Martinez-Caballero,J.A.Hermoso,A.Rodriguez-Romero
Key ref:
S.Martínez-Caballero et al. (2014). Comparative study of two GH19 chitinase-like proteins from Hevea brasiliensis, one exhibiting a novel carbohydrate-binding domain.
Febs J
,
281
, 4535-4554.
PubMed id:
25104038
DOI:
10.1111/febs.12962
Date:
18-Sep-13
Release date:
27-Aug-14
PROCHECK
Headers
References
Protein chains
?
Q949H3
(CHI1_HEVBR) - Inactive chitinase-like protein 1 from Hevea brasiliensis
Seq:
Struc:
314 a.a.
241 a.a.
*
Key:
PfamA domain
Secondary structure
CATH domain
*
PDB and UniProt seqs differ at 1 residue position (black cross)
Enzyme reactions
Enzyme class:
E.C.3.2.1.14
- chitinase.
[IntEnz]
[ExPASy]
[KEGG]
[BRENDA]
Reaction:
Hydrolysis of the 1,4-beta-linkages of N-acetyl-D-glucosamine polymers of chitin.
DOI no:
10.1111/febs.12962
Febs J
281
:4535-4554 (2014)
PubMed id:
25104038
Comparative study of two GH19 chitinase-like proteins from Hevea brasiliensis, one exhibiting a novel carbohydrate-binding domain.
S.Martínez-Caballero,
P.Cano-Sánchez,
I.Mares-Mejía,
A.G.Díaz-Sánchez,
M.L.Macías-Rubalcava,
J.A.Hermoso,
A.Rodríguez-Romero.
ABSTRACT
No abstract given.
'); } }