Structure of PDB 6a0l Chain A

Receptor sequence
>6a0lA (length=437) Species: 1665 (Arthrobacter globiformis) [Search protein sequence]
PDWLADAVFYQIFPERFANADPSLDPQNVVPWGSTPTPDNFFGGDLQGII
DHLDHIVALGANALYLTPIFEADTNHRYDAKDYFSIDHRLGTLETFHALM
AECRARGIRIVLDAVLNHCGDGHWAFADVVENEADSAYVNWFSVEGFPVT
AHPTPNYRTCSGCYYLPKWNAYNPEVRHHHLDVARYWIDQGIDGWRLDVP
YFINHTFWREFRTAVKGKSEDLYIVAEEWRSPVEWLQGDTADGTMNYTAR
DLILGFTADGGIDASALAAGLNALHAEIPAGFHRGMLNLLGSHDTERVLT
RHAGDVEAALLSYALLFSLEGAPMVYYGDEVGLTGDNDPGCRGAMPWNEE
SWNTRLLDGIRTFAAFRAHQPAMRRGRQTAVALDADTIAIVRSGERAAVI
VHRGEGTTVDTASIPELAPLDADTVVLGPLGTASLAT
3D structure
PDB6a0l Structural features of a bacterial cyclic alpha-maltosyl-(1→6)-maltose (CMM) hydrolase critical for CMM recognition and hydrolysis.
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D116 R199 D201 E230 H296 D297
Catalytic site (residue number reindexed from 1) D113 R196 D198 E227 H293 D294
Enzyme Commision number ?
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 Y81 H121 D201 E230 H296 D297 Y78 H118 D198 E227 H293 D294
BS02 GLC A H79 Y81 D341 R345 H76 Y78 D338 R342
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
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:6a0l, PDBe:6a0l, PDBj:6a0l
PDBsum6a0l
PubMed30181215
UniProtD2YYE1

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