Structure of PDB 5h4r Chain A

Receptor sequence
>5h4rA (length=375) Species: 1214564 (Caldicellulosiruptor sp. F32) [Search protein sequence]
RAKIPEIKIASRKIPNNAALKFVKDMKIGWNLGNTFDAAFENPSFDDELL
YETAWCGVKTTKQMIDTVKKAGFNTIRIPVSWHNHVTGSNFTISKRWLDR
VQQVVDYAMKNKMYVIINIHHDIMPGYYYPNSQHLQTSIKYVKSIWTQVA
TRFKNYNDHLIFEAVNQPRLTGSRFEWWLDMNNPECRDAVEAINKLNQVF
VDTVRSTGGNNVSRYLMVPGYAAAPEYVLIDEFKIPKDSSKYKNRIIISV
HAYRPYNFALQAPNESGSVSEWSVNSEESRRDIDYFMDKLYDKFVSKGIP
VVIGEFGARDKNGNLQSRVEFAAYYVRAARARGITCCWWDNNAFYGNGEN
FGLLDRKTLKWVYPEIVSAMMKYAR
3D structure
PDB5h4r Structural insights into the substrate specificity of a glycoside hydrolase family 5 lichenase from Caldicellulosiruptor sp. F32
ChainA
Resolution1.7031 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.4: cellulase.
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 BGC A Q188 W198 Y274 L281 Q167 W177 Y253 L260
BS02 BGC A H141 H142 N187 Q188 Y274 E326 W360 E370 H120 H121 N166 Q167 Y253 E305 W339 E349
BS03 BGC A N55 W76 H142 W360 N362 E370 N34 W55 H121 W339 N341 E349
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
Biological Process
GO:0000272 polysaccharide catabolic process
GO:0009251 glucan catabolic process
Cellular Component
GO:0005576 extracellular region
GO:0009986 cell surface

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Cellular Component
External links
PDB RCSB:5h4r, PDBe:5h4r, PDBj:5h4r
PDBsum5h4r
PubMed28838949
UniProtR9RX81

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