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
1bb3
Contents
Protein chains
130 a.a.
*
Waters
×291
*
Residue conservation analysis
PDB id:
1bb3
Links
PDBe
RCSB
SRS
MMDB
JenaLib
OCA
PDBWiki
Proteopedia
CATH
SCOP
FSSP
HSSP
PDBSWS
PQS
CSA
ProSAT
EDS
Whatcheck
Name:
Hydrolase
Title:
Human lysozyme mutant a96l
Structure:
Lysozyme. Chain: a, b. Engineered: yes. Mutation: yes
Source:
Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
Resolution:
1.80Å
R-factor:
0.188
R-free:
0.231
Authors:
A.G.Headley,S.M.Roe,L.H.Pearl
Date:
28-Apr-98
Release date:
12-Aug-98
PROCHECK
Headers
References
Protein chains
?
P61626
(LYSC_HUMAN) - Lysozyme C
Seq:
Struc:
148 a.a.
130 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.3.2.1.17
- Lysozyme.
[IntEnz]
[ExPASy]
[KEGG]
[BRENDA]
Reaction:
Hydrolysis of the 1,4-beta-linkages between N-acetyl-D-glucosamine and N-acetylmuramic acid in peptidoglycan heteropolymers of the prokaryotes cell walls.
Gene Ontology (GO) functional annotation
Cellular component
extracellular region
2 terms
Biological process
metabolic process
5 terms
Biochemical function
catalytic activity
5 terms