Structure of PDB 4az5 Chain A

Receptor sequence
>4az5A (length=434) Species: 170187 (Streptococcus pneumoniae TIGR4) [Search protein sequence]
NEKLAKKKIVSIDAGRKYFSPEQLKEIIDKAKHYGYTDLHLLVGNDGLRF
MLDDMSITANGKTYASDDVKRAIEKGTNDYYNDPNGNHLTESQMTDLINY
AKDKGIGLIPTVNSPGHMDAILNAMKELGIQNPNFSYFGKKSARTVDLDN
EQAVAFTKALIDKYAAYFAKKTEIFNIGLDEYANDATDAKGWSVLQADKY
YPNEGYPVKGYEKFIAYANDLARIVKSHGLKPMAFNDGIYYNSDTSFGSF
DKDIIVSMWTGGWGGYDVASSKLLAEKGHQILNTNDAWYYVLGRNADGQG
WYNLDQGLNGIKNTPITSVPKTEGADIPIIGGMVAAWADTPSARYSPSRL
FKLMRHFANANAEYFAADYESAEQALNEVPKDLNRYTAESVTAVKEAEKA
IRSLDSNLSRAQQDTIDQAIAKLQETVNNLTLTP
3D structure
PDB4az5 Inhibition of the Family 20 Glycoside Hydrolase Catalytic Modules in the Streptococcus Pneumoniae Exo-Beta-D-N-Acetylglucosaminidase, Strh.
ChainA
Resolution1.73 Å
3D
structure
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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 NGW A R196 H297 D360 E361 F415 W439 Y469 Y482 W517 D519 R16 H117 D180 E181 F235 W259 Y289 Y302 W337 D339 MOAD: Kd=1.02uM
PDBbind-CN: -logKd/Ki=5.99,Kd=1.02uM
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4az5, PDBe:4az5, PDBj:4az5
PDBsum4az5
PubMed24132305
UniProtP49610|STRH_STRPN Beta-N-acetylhexosaminidase (Gene Name=strH)

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