Structure of PDB 1gcy Chain A Binding Site BS02
Receptor Information
>1gcy 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
1gcy Chain A Residue 529 [
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Receptor-Ligand Complex Structure
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PDB
1gcy
Crystallization and structural analysis of intact maltotetraose-forming exo-amylase from Pseudomonas stutzeri.
Resolution
1.6 Å
Binding residue
(original residue number in PDB)
D1 Q2 H13 D16 E17
Binding residue
(residue number reindexed from 1)
D1 Q2 H13 D16 E17
Annotation score
4
Enzymatic activity
Catalytic site (original residue number in PDB)
R191 D193 E219 H293 D294
Catalytic site (residue number reindexed from 1)
R188 D190 E216 H290 D291
Enzyme Commision number
3.2.1.60
: glucan 1,4-alpha-maltotetraohydrolase.
Gene Ontology
Molecular Function
GO:0004556
alpha-amylase activity
GO:0016798
hydrolase activity, acting on glycosyl bonds
GO:0030246
carbohydrate binding
GO:0033910
glucan 1,4-alpha-maltotetraohydrolase activity
GO:0043169
cation binding
GO:0046872
metal ion binding
GO:2001070
starch binding
Biological Process
GO:0005975
carbohydrate metabolic process
GO:0005983
starch catabolic process
Cellular Component
GO:0005576
extracellular region
View graph for
Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:1gcy
,
PDBe:1gcy
,
PDBj:1gcy
PDBsum
1gcy
PubMed
11272837
UniProt
P13507
|AMT4_STUST Glucan 1,4-alpha-maltotetraohydrolase (Gene Name=amyP)
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