Structure of PDB 7byx Chain B Binding Site BS03
Receptor Information
>7byx Chain B (length=427) [
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NQIVSGAAWTDTAGNTIQAHGAGILQVGSTFYWFGEDKSHNSALFKAVSC
YTSSDLVNWSRQNDALSPIAGTMISTSNVVERPKVIFNQKNSEYVMWFHS
DSSNYGAAMVGVATAKTPCGPYTYKGSFKPLGADSRDESIFQDDDSAQTA
YLLYASDNNQNFKISRLDANYYNVTAQVSVMNGATLAAPGIVKHNGEYFL
IASHTSGWAPNPNKWFSASSLAGPWSAQQDIAPSATRTWYSQNAFDLPLG
SNAIYMGDRWRPSLLGSSRYIWYPLDFSSGAPQIVHADVWSVNVQAGTYS
VASGTSYEAENGQRGGSSTILSGSGFSGGKAVGYLGHGGTVTINNVQSNG
GSHWVALYFANGDSTYRNVTVSVNGGPSVLVDQPDSGGGNVVISVPVKLN
LNSGENSITFGSGQSNYAADLDKIIVY
Ligand information
Ligand ID
CA
InChI
InChI=1S/Ca/q+2
InChIKey
BHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Ca+2]
Formula
Ca
Name
CALCIUM ION
ChEMBL
DrugBank
DB14577
ZINC
PDB chain
7byx Chain B Residue 508 [
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Receptor-Ligand Complex Structure
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PDB
7byx
Unique active-site and subsite features in the arabinogalactan-degrading GH43 exo-beta-1,3-galactanase from Phanerochaete chrysosporium .
Resolution
2.3 Å
Binding residue
(original residue number in PDB)
E329 E331 S348 K351 D443
Binding residue
(residue number reindexed from 1)
E308 E310 S327 K330 D422
Annotation score
4
Enzymatic activity
Enzyme Commision number
3.2.1.145
: galactan 1,3-beta-galactosidase.
Gene Ontology
Molecular Function
GO:0004553
hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798
hydrolase activity, acting on glycosyl bonds
GO:0030246
carbohydrate binding
GO:0033943
galactan 1,3-beta-galactosidase activity
GO:0046872
metal ion binding
Biological Process
GO:0005975
carbohydrate metabolic process
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Molecular Function
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Biological Process
External links
PDB
RCSB:7byx
,
PDBe:7byx
,
PDBj:7byx
PDBsum
7byx
PubMed
33093171
UniProt
Q50KB2
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