Structure of PDB 2amg Chain A Binding Site BS01
Receptor Information
>2amg Chain A (length=415) Species:
316
(Stutzerimonas stutzeri) [
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DQAGKSPNAVRYHGGDEIILQGFHWNVVREAPNDWYNILRQQAATIAADG
FSAIWMPVPWRDFSSWSKSGGGEGYFWHDFNKNGRYGSDAQLRQAASALG
GAGVKVLYDVVPNHMNRGYPDKEINLPAGQGFWRNDCADPGNYPNDCDDG
DRFIGGDADLNTGHPQVYGMFRDEFTNLRSQYGAGGFRFDFVRGYAPERV
NSWMTDSADNSFCVGELWKGPSEYPNWDWRNTASWQQIIKDWSDRAKCPV
FDFALKERMQNGSIADWKHGLNGNPDPRWREVAVTFVDNHDTGYSPGQNG
GQHHWALQDGLIRQAYAYILTSPGTPVVYWDHMYDWGYGDFIRQLIQVRR
AAGVRADSAISFHSGYSGLVATVSGSQQTLVVALNSDLGNPGQVASGSFS
EAVNASNGQVRVWRS
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
2amg Chain A Residue 451 [
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Receptor-Ligand Complex Structure
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PDB
2amg
Crystal structure of a maltotetraose-forming exo-amylase from Pseudomonas stutzeri.
Resolution
2.0 Å
Binding residue
(original residue number in PDB)
N116 D151 D154 D162 G197
Binding residue
(residue number reindexed from 1)
N113 D148 D151 D159 G194
Annotation score
4
Enzymatic activity
Catalytic site (original residue number in PDB)
D193 E219 D294
Catalytic site (residue number reindexed from 1)
D190 E216 D291
Enzyme Commision number
3.2.1.60
: glucan 1,4-alpha-maltotetraohydrolase.
Gene Ontology
Molecular Function
GO:0004556
alpha-amylase activity
GO:0043169
cation binding
Biological Process
GO:0005975
carbohydrate metabolic process
View graph for
Molecular Function
View graph for
Biological Process
External links
PDB
RCSB:2amg
,
PDBe:2amg
,
PDBj:2amg
PDBsum
2amg
PubMed
9126844
UniProt
P13507
|AMT4_STUST Glucan 1,4-alpha-maltotetraohydrolase (Gene Name=amyP)
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