Structure of PDB 4azg Chain B

Receptor sequence
>4azgB (length=414) Species: 170187 (Streptococcus pneumoniae TIGR4) [Search protein sequence]
RGSHMEKLAKNKVISIDAGRKYFTLNQLKRIVDKASELGYSDVHLLLGND
GLRFLLDDMTITANGKTYASDDVKKAIIEGTKAYYDDPNGTALTQAEVTE
LIEYAKSKDIGLIPAINSPGHMDAMLVAMEKLGIKNPQAHFDKVSKTTMD
LKNEEAMNFVKALIGKYMDFFAGKTKIFNFGTDEYANDATSAQGWYYLKW
YQLYGKFAEYANTLAAMAKERGLQPMAFNDGFYYEDKDDVQFDKDVLISY
WSKGWWGYNLASPQYLASKGYKFLNTNGDWYYILGQKPEDGGGFLKKAIE
NTGKTPFNQLASTKYPEVDLPTVGSMLSIWADRPSAEYKEEEIFELMTAF
ADHNKDYFRANYNALREELAKIPYSKESLEALDAAKTALNYNLNRNKQAE
LDTLVANLKAALQG
3D structure
PDB4azg Inhibition of the Family 20 Glycoside Hydrolase Catalytic Modules in the Streptococcus Pneumoniae Exo-Beta-D-N-Acetylglucosaminidase, Strh.
ChainB
Resolution2.4 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 OAN B R641 D804 E805 F849 W872 W876 Y879 Y902 I904 W951 D953 R20 D183 E184 F228 W251 W255 Y258 Y281 I283 W330 D332 MOAD: Kd=79.05nM
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
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Biological Process
External links
PDB RCSB:4azg, PDBe:4azg, PDBj:4azg
PDBsum4azg
PubMed24132305
UniProtP49610|STRH_STRPN Beta-N-acetylhexosaminidase (Gene Name=strH)

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