Structure of PDB 4zfm Chain C

Receptor sequence
>4zfmC (length=461) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence]
HLKPFPPEFLWGAASAAYQVEGAWNEDGKGLSVWDVFAKQPGRTFKGTNG
DVAVDHYHRYQEDVALMAEMGLKAYRFSVSWSRVFPDGNGAVNEKGLDFY
DRLIEELRNHGIEPIVTLYHWDVPQALMDAYGAWESRRIIDDFDRYAVTL
FQRFGDRVKYWVTLNQQNIFISFGYRLGLHPPGVKDMKRMYEANHIANLA
NAKVIQSFRHYVPDGKIGPSFAYSPMYPYDSRPENVLAFENAEEFQNHWW
MDVYAWGMYPQAAWNYLESQGLEPTVAPGDWELLQAAKPDFMGVNYYQTT
TVEHNPPDGVGTSSGIPGLFKTVRNPHVDTTNWDWAIDPVGLRIGLRRIA
NRYQLPILITENGLGEFDTLEPGDIVNDDYRIDYLRRHVQEIQRAITDGV
DVLGYCAWSFTDLLSWLNGYQKRYGFVYVNRDDESEKDLRRIKKKSFYWY
QRVIETNGAEL
3D structure
PDB4zfm Structure of Gan1D-E170Q in complex with cellobiose-6-phosphate
ChainC
Resolution1.4 Å
3D
structure
Catalytic site residues are labeled in the 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
Catalytic site (original residue number in PDB) R80 H124 Q170 I173 N299 Y301 E378
Catalytic site (residue number reindexed from 1) R76 H120 Q166 I169 N295 Y297 E361
Enzyme Commision number 3.2.1.85: 6-phospho-beta-galactosidase.
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 0WK C Q23 H124 Q170 E378 W425 S432 W433 Y441 Q19 H120 Q166 E361 W408 S415 W416 Y424
BS02 BGC C Q170 Y301 Q166 Y297
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0008422 beta-glucosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0033920 6-phospho-beta-galactosidase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0016052 carbohydrate catabolic process
Cellular Component
GO:0005829 cytosol

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4zfm, PDBe:4zfm, PDBj:4zfm
PDBsum4zfm
PubMed
UniProtW8QF82

[Back to BioLiP]