Structure of PDB 5u2o Chain A

Receptor sequence
>5u2oA (length=543) Species: 717605 (Thermobacillus composti KWC4) [Search protein sequence]
MLPEFPKIAVVAGSEAESVFRVVDIGTGDVVYEGRLSDSVYDDASGDTVR
HADFGEWKRPGSYSVTVGRSSSAPFRIGNDVYRAPLIQAARSYTLARCGV
AIDDPVTGLRHDVCHAQDKQAMLFFEDPFHRQGDPIDVSGGWHDAGDYGK
YVPTGAVAAAQLMLAWEMRPELWRSLSLSLPAGLSEPERRAGLPDLLVEI
KYELDWLLRMQRPDGAVYLKVAGGAWPGYIRPEEDTADRYVFGLSTYGTA
QFAGAAAMGARVYAPFLPDYARKLLDAAIRAQRYLEQHPDPEFRYDEGQN
NGSGPYEKRTDREERFWAAAELLRTTDDARYDAYIREHFSDFLEGKTSAV
FWGNTVLLGQWAYVNAERADADHKASVRASLTAYADELVRWASANGYRSV
LRPTDYFWGSAREAMGRAQALLLADAVAPNRAYLETALDQAHWLFGRNAA
GTSFMTGIGMHSPQKPHHRLVASTQTLIPGLVVGGPNAQGGDPIMDRLLR
ESDPRVFPAKAYVDDWEAYSVNEPAIDYTAPAVFVLTRFAEDR
3D structure
PDB5u2o Engineering glycoside hydrolase stability by the introduction of zinc binding.
ChainA
Resolution1.46 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 ?
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 ZN A C98 C114 H115 H143 C98 C114 H115 H143
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0008810 cellulase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0046872 metal ion binding
Biological Process
GO:0000272 polysaccharide catabolic process
GO:0005975 carbohydrate metabolic process

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:5u2o, PDBe:5u2o, PDBj:5u2o
PDBsum5u2o
PubMed29968680
UniProtA0A384E0U3

[Back to BioLiP]