Structure of PDB 5ohz Chain D

Receptor sequence
>5ohzD (length=442) Species: 1122247 (Mycolicibacterium hassiacum DSM 44199) [Search protein sequence]
PSFTPTQLAARAAYLLRGNDLGTMTTAAPLLYPHMWSWDAAFVAIGLAPL
SVERAVVELDTLLSAQWRNGMIPHIVFANGVDGYFPGPARWATATLADNA
PRNRLTSGITQPPVHAIAVQRILEHARTRGRSTRAVAEAFLDRRWGDLMR
WHRWLAECRDRNERGRITLYHGWESGMDNSPRWDSAYANVVPGKLPEYQR
ADNVIITDPSQRPSDGEYDRYLWLLEEMKAVRYDDERLPSVMSFQVEDVF
FSAIFSVACQVLAEIGEDYKRPHADVKDLYLWAERFRAGVVETTDQRTGA
ARDFDVLAEKWLVTETAAQFAPLLCGGLPHDRERALLKLLEGPRFCGHPD
LKYGLIPSTSPVSRDFRPREYWRGPVWPVLTWLFSWCFARRGWAERARLL
RQEGLRQASDGSFAEYYEPFTGEPLGSMQQSWTAAAVLDWLG
3D structure
PDB5ohz The structural characterization of a glucosylglycerate hydrolase provides insights into the molecular mechanism of mycobacterial recovery from nitrogen starvation.
ChainD
Resolution2.036 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 3.2.1.208: glucosylglycerate hydrolase.
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 SER D W40 Y88 D182 R216 Y375 W36 Y84 D178 R212 Y371
Gene Ontology
Molecular Function
GO:0004573 Glc3Man9GlcNAc2 oligosaccharide glucosidase activity
GO:0016787 hydrolase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0102547 glucosylglycerate hydrolase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006487 protein N-linked glycosylation
GO:0009311 oligosaccharide metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5ohz, PDBe:5ohz, PDBj:5ohz
PDBsum5ohz
PubMed31316802
UniProtK5BDL0|GGH_MYCHD Glucosylglycerate hydrolase (Gene Name=ggh)

[Back to BioLiP]