Structure of PDB 4gvh Chain A

Receptor sequence
>4gvhA (length=341) Species: 99287 (Salmonella enterica subsp. enterica serovar Typhimurium str. LT2) [Search protein sequence]
MGPVMLNVEGCELDAEEREILAHPLVGGLILFTRNYHDPEQLRELVRQIR
AASRNHLVVAVDQEGGRVQRFREGFTRLPAAQSFFALHGLEEGGRLAQEA
GWLMASEMIAMDIDISFAPVLDVGHISAAIGERSYHADPAKALAMATRFI
DGMHDAGMKTTGKHFPGHGAVTADSHKETPCDPRPETDIRGKDMSVFRTL
ISENKLDAIMPAHVIYRAIDPRPASGSPYWLKTVLRQELGFDGVIFSDDL
SMEGAAIMGSYAERAQASLDAGCDMILVCNNRKGAVSVLDNLSPIKAERV
TRLYHKGSFSRRELMDSARWKTASAQLNQLHERWQEEKAGH
3D structure
PDB4gvh Active Site Plasticity within the Glycoside Hydrolase NagZ Underlies a Dynamic Mechanism of Substrate Distortion.
ChainA
Resolution1.45 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 3.2.1.52: beta-N-acetylhexosaminidase.
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 0XY A I30 D62 R133 K163 H164 M210 D248 I30 D62 R133 K163 H164 M210 D248
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004563 beta-N-acetylhexosaminidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0008360 regulation of cell shape
GO:0009252 peptidoglycan biosynthetic process
GO:0009254 peptidoglycan turnover
GO:0046677 response to antibiotic
GO:0051301 cell division
GO:0071555 cell wall organization
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:4gvh, PDBe:4gvh, PDBj:4gvh
PDBsum4gvh
PubMed23177201
UniProtQ8ZQ06|NAGZ_SALTY Beta-hexosaminidase (Gene Name=nagZ)

[Back to BioLiP]