Structure of PDB 1lwj Chain B

Receptor sequence
>1lwjB (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
ChainB
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D530 R625 D627 E657 H718 D719
Catalytic site (residue number reindexed from 1) D89 R184 D186 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 B H535 W572 F591 D627 A628 K630 H631 E657 W659 H718 D719 H94 W131 F150 D186 A187 K189 H190 E216 W218 H277 D278
BS02 CA B D454 N456 D458 V460 D462 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

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

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