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
Go to PDB code:
Hydrolase
PDB id
1ihd
Contents
Protein chains
307 a.a.
*
Waters
×54
*
Residue conservation analysis
PDB id:
1ihd
Links
PDBe
RCSB
SRS
MMDB
JenaLib
OCA
PDBWiki
Proteopedia
CATH
SCOP
FSSP
HSSP
PDBSWS
PQS
CSA
ProSAT
Whatcheck
Name:
Hydrolase
Title:
Crystal structure of trigonal form of d90e mutant of escheri asparaginase ii
Structure:
L-asparaginase ii. Chain: a, c. Synonym: l-asnase ii. Engineered: yes. Mutation: yes
Source:
Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit:
Tetramer (from PDB file)
Resolution:
2.65Å
R-factor:
0.169
R-free:
0.209
Authors:
D.Borek,M.Jaskolski
Key ref:
D.Borek and m.jaskolski Structure analysis of d90e mutant of e.Coli asparaginase ii in three crystal forms.
To be published
,
Date:
19-Apr-01
Release date:
09-Sep-03
PROCHECK
Headers
References
Protein chains
?
P00805
(ASPG2_ECOLI) - L-asparaginase 2
Seq:
Struc:
348 a.a.
307 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.3.5.1.1
- Asparaginase.
[IntEnz]
[ExPASy]
[KEGG]
[BRENDA]
Reaction:
L-asparagine + H
2
O = L-aspartate + NH
3
L-asparagine
+
H(2)O
=
L-aspartate
+
NH(3)
Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
Gene Ontology (GO) functional annotation
Cellular component
periplasmic space
2 terms
Biological process
cellular amino acid metabolic process
2 terms
Biochemical function
hydrolase activity
2 terms