Structure of PDB 5a94 Chain B

Receptor sequence
>5a94B (length=336) Species: 203122 (Saccharophagus degradans 2-40) [Search protein sequence]
DWWDIPYPSQFDVKSLKTQSFISVKGNKFIDDKGKTFTFRGVNIADTGKL
LSRNQWQKSLFEELANNWGVNTIRLPIHPVSWRKLGPDVYLGHIDEAVRW
ANDLGIYLILDWHSIGYLPTEQYQHPMYDTTIKETRDFWRRITFRYQNVP
TVAVYELFNEPTTMGNTLGERNWAEWKTLNESLIDMIYASDKTVIPLVAG
FNWAYDLSPIKKAPIEREGIAYAAHPYPQKAKPEVKNDKNFFKLWDEKWG
FAADTYPVIATQLGWVQPDGYGAHIPVKDDGSYGPRIVKYMQKKGVSYTV
WVFDPDWSPTMINDWDFTPSEQGAFFKQVMLEAKKR
3D structure
PDB5a94 The Quaternary Structure of a Glycoside Hydrolase Dictates Specificity Towards Beta-Glucans
ChainB
Resolution1.99 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.73: licheninase.
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 B H142 I144 E189 Q291 H303 W330 S337 H113 I115 E160 Q262 H274 W301 S308
BS02 BGC B H107 M156 Y157 W336 S337 H78 M127 Y128 W307 S308
BS03 BGC B Y300 W336 Y271 W307
BS04 MG B V178 V181 V149 V152
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0000272 polysaccharide catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:5a94, PDBe:5a94, PDBj:5a94
PDBsum5a94
PubMed26755730
UniProtQ21KE5

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