Structure of PDB 1obb Chain A

Receptor sequence
>1obbA (length=478) Species: 243274 (Thermotoga maritima MSB8) [Search protein sequence]
PSVKIGIIGAGSAVFSLRLVSDLCKTPGLSGSTVTLMDIDEERLDAILTI
AKKYVEEVGADLKFEKTMNLDDVIIDADFVINTAMVGGHTYLEKVRQIGE
KYGYYRGIDAQEFNMVSDYYTFSNYNQLKYFVDIARKIEKLSPKAWYLQA
ANPIFEGTTLVTRTVPIKAVGFCHGHYGVMEIVEKLGLEEEKVDWQVAGV
NHGIWLNRFRYNGGNAYPLLDKWIEEKSKDWKPENPFNDQLSPAAIDMYR
FYGVMPIGDTVRNSSWRYHRDLETKKKWYGEPWGGADSEIGWKWYQDTLG
KVTEITKKVAKFIKENPSVRLSDLGSVLGKDLSEKQFVLEVEKILDPERK
SGEQHIPFIDALLNDNKARFVVNIPNKGIIHGIDDDVVVEVPALVDKNGI
HPEKIEPPLPDRVVKYYLRPRIMRMEMALEAFLTGDIRIIKELLYRDPRT
KSDEQVEKVIEEILALPENEEMRKHYLK
3D structure
PDB1obb Crystal Structure of Thermotoga Maritima Alpha-Glucosidase Agla Defines a New Clan of Nad+-Dependent Glycosidases
ChainA
Resolution1.9 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.20: alpha-glucosidase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 GLC A D119 N153 H175 H203 D260 R263 W293 Y296 D118 N152 H174 H202 D259 R262 W292 Y295
BS02 NAD A G10 G12 M38 D39 I40 R44 T84 A85 M86 H90 D119 Y131 A152 N153 Y296 G9 G11 M37 D38 I39 R43 T83 A84 M85 H89 D118 Y130 A151 N152 Y295
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004558 alpha-1,4-glucosidase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0016798 hydrolase activity, acting on glycosyl bonds
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:1obb, PDBe:1obb, PDBj:1obb
PDBsum1obb
PubMed12588867
UniProtO33830|AGLA_THEMA Alpha-glucosidase (Gene Name=aglA)

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