Structure of PDB 4bs0 Chain B

Receptor sequence
>4bs0B (length=299) Species: 5087 (Thermoascus aurantiacus) [Search protein sequence]
QSIDQLIKARGKVYFGVATDQNRLTTGKNAAIIKADFGMVWPENSMQWDA
TEPSQGNFNFAGADYLVNWAQQNGKLIGAGCLVWHNFLPSWVSSITDKNT
LINVMKNHITTLMTRYKGKIRTWDVVGEAFNEDGSLRQNVFLNVIGEDYI
PIAFQTARAADPNAKLYIMDYNLDSASYPKTQAIVNRVKQWRAAGVPIDG
IGSQMHLSAGQGAGVLQALPLLASAGTPEVSILMLDVAGASPTDYVNVVN
ACLNVQSCVGITVMGVADPDSAFASSTPLLFDGNFNPKPAYNAIVQDLQ
3D structure
PDB4bs0 Precision is Essential for Efficient Catalysis in an Evolved Kemp Eliminase
ChainB
Resolution1.09 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E131 M172 H209 M237 D239
Catalytic site (residue number reindexed from 1) E128 M169 H206 M234 D236
Enzyme Commision number 3.2.1.8: endo-1,4-beta-xylanase.
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 6NT B W44 G83 C84 D127 L236 M237 T265 M267 W41 G80 C81 D124 L233 M234 T262 M264 MOAD: Ki=2uM
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0031176 endo-1,4-beta-xylanase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0045493 xylan catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4bs0, PDBe:4bs0, PDBj:4bs0
PDBsum4bs0
PubMed24132235
UniProtP23360|XYNA_THEAU Endo-1,4-beta-xylanase (Gene Name=XYNA)

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