Structure of PDB 3ut0 Chain A Binding Site BS01

Receptor Information
>3ut0 Chain A (length=804) Species: 368972 (Pseudoalteromonas sp. BB1) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
QVNWPYVNTKLKRDPAVEAQIEKLLAKMTIEQKVAQMIQPEIGYLTVEQM
RKYGFGSYLNGGNTAPYGNKRADQATWLKYADEMYLAAMDSTLDGIAIPT
VWGTDAMHGHSNVYGATLFPHNIGLGAARDTDLIKRIGQATAKEVAATGI
EWSFAPTVAVVRDDRWGRTYESYSEDPDLVKRYAGEMVTGIQGDVGADFL
KGSNRIATAKHFVGDGGTERGVDRGNTLIDEKGLRDIHSAGYFSAINQGV
QSVMASFNSWNGKRVHGDKHLLTDVLKNQLGFDGFVVSDWNAHKFVEGCD
LEQCAQAINAGVDVIMVPEHFEAFYHNTVKQVKAGVIAESRINDAVRRFL
RAKIRWGVFTKSKPSARPESQHPQWLGAAEHRTLAREAVRKSLVLLKNNE
SILPIKASSRILVAGKGANAINMQAGGWSVSWQGTDNTNSDFPNATSIFS
GLQSQVTKAGGKITLSESGEYTSKPDVAIVVIGEEPYAEWFGDIELLEFQ
HETKHALALLKQLKADNIPVVTVFLSGRPLWVNKELNASDAFVAAWLPGS
EGEGVADVLLTNKQGKTQFDFTGKLSFSWPKYDDQFTLNLNDADYDPLFA
YGYGLTYQDNINVPVLSEKTSPSDSHPLFVRSLAKNMTWQLADTSTQKVL
ASGASATSGDKQSLLMQSVNLSYQEDGRGFNWRAQAALSLSYLEPTPLDS
KFSTGYLELKMRIDKAPEQGANLQVMCSESNCLRDIDFSSFSQLMADKSW
HTLAIPLHCDDSEQPITDALRITSQNLSLAIADVALTIKPSDDSISLTCA
KLEH
Ligand information
Ligand IDCA
InChIInChI=1S/Ca/q+2
InChIKeyBHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Ca+2]
FormulaCa
NameCALCIUM ION
ChEMBL
DrugBankDB14577
ZINC
PDB chain3ut0 Chain A Residue 901 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB3ut0 Structure and activity of exo-1,3/1,4-beta-glucanase from marine bacterium Pseudoalteromonas sp. BB1 showing a novel C-terminal domain
Resolution2.3 Å
Binding residue
(original residue number in PDB)
E179 L592 N593
Binding residue
(residue number reindexed from 1)
E175 L588 N589
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) D293 E493
Catalytic site (residue number reindexed from 1) D289 E489
Enzyme Commision number 3.2.1.21: beta-glucosidase.
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
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0009251 glucan catabolic process

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:3ut0, PDBe:3ut0, PDBj:3ut0
PDBsum3ut0
PubMed22129429
UniProtQ0QJA3

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