Structure of PDB 2gjp Chain A Binding Site BS01

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 IDBGC
InChIInChI=1S/C6H12O6/c7-1-2-3(8)4(9)5(10)6(11)12-2/h2-11H,1H2/t2-,3-,4+,5-,6-/m1/s1
InChIKeyWQZGKKKJIJFFOK-VFUOTHLCSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6C(C1C(C(C(C(O1)O)O)O)O)O
CACTVS 3.370OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O
CACTVS 3.370OC[CH]1O[CH](O)[CH](O)[CH](O)[CH]1O
OpenEye OEToolkits 1.7.6C([C@@H]1[C@H]([C@@H]([C@H]([C@@H](O1)O)O)O)O)O
ACDLabs 12.01OC1C(O)C(OC(O)C1O)CO
FormulaC6 H12 O6
Namebeta-D-glucopyranose;
beta-D-glucose;
D-glucose;
glucose
ChEMBLCHEMBL1614854
DrugBankDB02379
ZINCZINC000003833800
PDB chain2gjp Chain B Residue 1 [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)		N270 Y295
Binding residue
(residue number reindexed from 1)		N266 Y291
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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