Structure of PDB 3bcf Chain A Binding Site BS01

Receptor Information
>3bcf Chain A (length=585) Species: 373903 (Halothermothrix orenii H 168) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SLFLIESEPSTGASVSKNLTEIILIFSNDINKVSQLALTDLITDSDIQGI
DYNIEGNKVIINNFSLEPTCNYRLSYEVIDIYDNHLQGYIEFLVNQSNYP
QIPDQEVNHTILQAFYWEMNTGEYATEHPEEANLWNLLAERAPELAEAGF
TAVWLPPANKGMAGIHDVGYGTYDLWDLGEFDQKGTVRTKYGTKGELENA
IDALHNNDIKVYFDAVLNHRMGADYAETVLLDENSRDKPGQYIKAWTGFN
FPGRNGEYSNFTWNGQCFDGTDWDDYSKESGKYLFDEKSWDWTYNWDEDY
LMGADVDYENEAVQNDVIDWGQWIINNIDFDGFRLDAVKHIDYRFIDKWM
SAVQNSSNRDVFFVGEAWVEDVDDLKGFLDTVGNPDLRVFDFPLRSFFVD
MLNGAYMADLRNAGLVNSPGYENRAVTFVDNHDTDRDEGSYTVSIYSRKY
QAYAYILTRAEGVPTVYWKDYYIWEMKEGLDKLLTARRYYAYGPGYEVDN
NDADIYSYVRSGFPDVAGDGLVLMISDGTSGNVAGKWINSRQPDTEFYDL
TGHIKEHVTTDSEGYGNFKVIKSEDKGWSIWVPVE
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 chain3bcf Chain A Residue 701 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3bcf Crystal Structure of the Polyextremophilic alpha-Amylase AmyB from Halothermothrix orenii: Details of a Productive Enzyme-Substrate Complex and an N Domain with a Role in Binding Raw Starch
Resolution2.3 Å
Binding residue
(original residue number in PDB)		D283 S303 D305 D321 E323
Binding residue
(residue number reindexed from 1)		D269 S289 D291 D307 E309
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) D350 E380 D447
Catalytic site (residue number reindexed from 1) D336 E366 D433
Enzyme Commision number 3.2.1.98: glucan 1,4-alpha-maltohexaosidase.
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0033927 glucan 1,4-alpha-maltohexaosidase 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:3bcf, PDBe:3bcf, PDBj:3bcf
PDBsum3bcf
PubMed18387632
UniProtB8CZ54

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