Structure of PDB 4azc Chain B

Receptor sequence
>4azcB (length=421) Species: 170187 (Streptococcus pneumoniae TIGR4) [Search protein sequence]
GSHMEKLAKNKVISIDAGRKYFTLNQLKRIVDKASELGYSDVHLLLGNDG
LRFLLDDMTITANGKTYASDDVKKAIIEGTKAYYDDPNGTALTQAEVTEL
IEYAKSKDIGLIPAINSPGHMDAMLVAMEKLGIKNPQAHFDKVSKTTMDL
KNEEAMNFVKALIGKYMDFFAGKTKIFNFGTDEYANDATSAQGWYYLKWY
QLYGKFAEYANTLAAMAKERGLQPMAFNDGFYYEDKDDVQFDKDVLISYW
SKGWWGYNLASPQYLASKGYKFLNTNGDWYYILGQKPEDGGGFLKKAIEN
TGKTPFNQLASTKYPEVDLPTVGSMLSIWADRPSAEYKEEEIFELMTAFA
DHNKDYFRANYNALREELAKIPTNLEGYSKESLEALDAAKTALNYNLNRN
KQAELDTLVANLKAALQGLKP
3D structure
PDB4azc Inhibition of the Family 20 Glycoside Hydrolase Catalytic Modules in the Streptococcus Pneumoniae Exo-Beta-D-N-Acetylglucosaminidase, Strh.
ChainB
Resolution2.09 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 NGW B R641 D804 E805 F849 W872 Y902 I904 W951 D953 R19 D182 E183 F227 W250 Y280 I282 W329 D331 MOAD: Kd=1.38uM
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0005975 carbohydrate metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4azc, PDBe:4azc, PDBj:4azc
PDBsum4azc
PubMed24132305
UniProtP49610|STRH_STRPN Beta-N-acetylhexosaminidase (Gene Name=strH)

[Back to BioLiP]