Structure of PDB 6a0k Chain B

Receptor sequence
>6a0kB (length=442) Species: 1665 (Arthrobacter globiformis) [Search protein sequence]
TAPDWLADAVFYQIFPERFANADPSLDPQNVVPWGSTPTPDNFFGGDLQG
IIDHLDHIVALGANALYLTPIFEADTNHRYDAKDYFSIDHRLGTLETFHA
LMAECRARGIRIVLDAVLNHCGDGHWAFADVVENEADSAYVNWFSVEGFP
VTAHPTPNYRTCSGCYYLPKWNAYNPEVRHHHLDVARYWIDQGIDGWRLD
VPYFINHTFWREFRTAVKGKSEDLYIVAEEWRSPVEWLQGDTADGTMNYT
ARDLILGFTADGGIDASALAAGLNALHAEIPAGFHRGMLNLLGSHDTERV
LTRHAGDVEAALLSYALLFSLEGAPMVYYGDEVGLTGDNDPGCRGAMPWN
EESWNTRLLDGIRTFAAFRAHQPAMRRGRQTAVALDADTIAIVRSGGDER
AAVIVHRGEGTTVDTASIPELAPLDADTVVLGPLGTASLATA
3D structure
PDB6a0k Structural features of a bacterial cyclic alpha-maltosyl-(1→6)-maltose (CMM) hydrolase critical for CMM recognition and hydrolysis.
ChainB
Resolution1.94 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) D115 R198 D200 E229 H295 D296
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 B Y81 H121 R199 D201 V202 E230 H296 D297 Y80 H120 R198 D200 V201 E229 H295 D296
BS02 GLC B H79 Y81 D341 R345 H78 Y80 D340 R344
BS03 GLC B C163 S164 C162 S163
BS04 BGC B E231 W232 E230 W231
BS05 GLC B Y204 F205 W232 Y203 F204 W231
BS06 CA B N22 D24 D28 G46 D48 N21 D23 D27 G45 D47
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:6a0k, PDBe:6a0k, PDBj:6a0k
PDBsum6a0k
PubMed30181215
UniProtD2YYE1

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