Structure of PDB 2gjp Chain A Binding Site BS12

Receptor Information
>2gjp Chain A (length=481) Species: 79882 (Sutcliffiella halmapala) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TNGTMMQYFEWHLPNDGQHWNRLRDDASNLRNRGITAIWIPPAWKGTSQN
DVGYGAYDLYDLGEFNQKGTVRTKYGTRSQLESAIHALKNNGVQVYGDVV
MNHKGGADATENVLAVEVNPNNRNQEISGDYTIEAWTKFDFPGRGNTYSD
FKWRWYHFDGVDWDQSRQFQNRIYKFRGDGKAWDWEVDSENGNYDYLMYA
DVDMDHPEVVNELRRWGEWYTNTLNLDGFRIDAVKHIKYSFTRDWLTHVR
NATGKEMFAVAEFWKNDLGALENYLNKTNWNHSVFDVPLHYNLYNASNSG
GNYDMAKLLNGTVVQKHPMHAVTFVDNHDSQPGESLESFVQEWFKPLAYA
LILTREQGYPSVFYGDYYGIPTHSVPAMKAKIDPILEARQNFAYGTQHDY
FDHHNIIGWTREGNTTHPNSGLATIMSDGPGGEKWMYVGQNKAGQVWHDI
TGNKPGTVTINADGWANFSVNGGSVSIWVKR
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 chain2gjp Chain A Residue 1487 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2gjp Structure of Bacillus halmapalus alpha-amylase crystallized with and without the substrate analogue acarbose and maltose.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		D163 A186 D188 D207 D209
Binding residue
(residue number reindexed from 1)		D159 A182 D184 D203 D205
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) D236 E266 D333
Catalytic site (residue number reindexed from 1) D232 E262 D329
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:0004556 alpha-amylase activity
GO:0005509 calcium ion binding
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0033927 glucan 1,4-alpha-maltohexaosidase activity
GO:0043169 cation binding
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0005983 starch catabolic process
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2gjp, PDBe:2gjp, PDBj:2gjp
PDBsum2gjp
PubMed16946462
UniProtP19571|AMT6_BACS7 Glucan 1,4-alpha-maltohexaosidase

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