Structure of PDB 1lwj Chain A

Receptor sequence
>1lwjA (length=441) Species: 2336 (Thermotoga maritima) [Search protein sequence]
MIGYQIYVRSFRDGNLDGVGDFRGLKNAVSYLKELGIDFVWLMPVFSSIS
FHGYDVVDFYSFKAEYGSEREFKEMIEAFHDSGIKVVLDLPIHHTGFLHT
WFQKALKGDPHYRDYYVWANKETDLDERREWDGEKIWHPLEDGRFYRGLF
GPFSPDLNYDNPQVFDEMKRLVLHLLDMGVDGFRFDAAKHMRDTIEQNVR
FWKYFLSDLKGIFLAEIWAEARMVDEHGRIFGYMLNFDTSHCIKEAVWKE
NTRVLIESIERAVIAKDYLPVNFTSNHDMSRLASFEGGFSKEKIKLSISI
LFTLPGVPLVFYGDELGMKGVYQKPNTEVVLDPFPWNESMCVEGQTFWKW
PAYNGPFSGISVEYQKRDPDSILSHTLGWTRFRKENQWIDRAKLEFLCKE
DKFLVYRLYDDQHSLKVFHNLSGEEVVFEGVKMKPYKTEVV
3D structure
PDB1lwj CRYSTAL STRUCTURE OF THERMOTOGA MARITIMA 4-ALPHA-GLUCANOTRANSFERASE AND ITS ACARBOSE COMPLEX: IMPLICATIONS FOR SUBSTRATE SPECIFICITY AND CATALYSIS
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D89 E216 H277 D278
Catalytic site (residue number reindexed from 1) D89 E216 H277 D278
Enzyme Commision number 2.4.1.25: 4-alpha-glucanotransferase.
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 ACG A Y54 H94 W131 F150 D186 A187 H190 E216 W218 H277 D278 Y54 H94 W131 F150 D186 A187 H190 E216 W218 H277 D278
BS02 CA A D13 N15 D17 V19 D21 D13 N15 D17 V19 D21
Gene Ontology
Molecular Function
GO:0004134 4-alpha-glucanotransferase activity
GO:0004556 alpha-amylase activity
GO:0016757 glycosyltransferase activity
GO:0043169 cation binding
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0009313 oligosaccharide catabolic process
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1lwj, PDBe:1lwj, PDBj:1lwj
PDBsum1lwj
PubMed12139940
UniProtP80099|MGTA_THEMA 4-alpha-glucanotransferase (Gene Name=mgtA)

[Back to BioLiP]