Structure of PDB 1gvi Chain B

Receptor sequence
>1gviB (length=588) Species: 275 (Thermus sp.) [Search protein sequence]
MRKEAIHHRSTDNFAYAYDSETLHLRLQTKKNDVDHVELLFGDPYEWHDG
AWQFQTMPMRKTGSDGLFDYWLAEVKPPYRRLRYGFVLRAGGEKLVYTEK
GFYHEAPSDDTAYYFCFPFLHRVDLFQAPDWVKDTVWYQIFPERFANGNP
AISPKGARPWGSEDPTPTSFFGGDLQGIIDHLDYLADLGITGIYLTPIFR
APSNHKYDTADYFEIDPHFGDKETLKTLVKRCHEKGIRVMLDAVFNHCGY
EFAPFQDVLKNGAASRYKDWFHIREFPLQTEPRPNYDTFAFVPHMPKLNT
AHPEVKRYLLDVATYWIREFDIDGWRLDVANEIDHQFWREFRQAVKALKP
DVYILGLIWHDAMPWLRGDQFDAVMNYPLADAALRFFAKEDMSASEFADR
LMHVLHSYPKQVNEAAFNLLGSHDTPRLLTVCGGDVRKVKLLFLFQLTFT
GSPCIYYGDEIGMTGGNDPECRKCMVWDPEKQNKELYEHVKQLIALRKQY
RALRRGDVAFLTADDEVNHLVYAKTDGNETVMIIINRSNEAAEIPMPIDA
RGKWLVNLLTGERFAAEAETLCVSLPPYGFVLYAVESW
3D structure
PDB1gvi Cyclomaltodextrinase, Neopullulanase, and Maltogenic Amylase are Nearly Indistinguishable from Each Other
ChainB
Resolution3.3 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) D242 R326 D328 L357 H423 D424
Catalytic site (residue number reindexed from 1) D242 R326 D328 L357 H423 D424
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 Y45 W47 Y45 W47
BS02 GLC B F289 W359 Y377 D424 F289 W359 Y377 D424
BS03 GLC B Y207 H247 F289 D328 H423 D424 Y207 H247 F289 D328 H423 D424
BS04 GLC B H205 R472 H205 R472
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0005975 carbohydrate metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1gvi, PDBe:1gvi, PDBj:1gvi
PDBsum1gvi
PubMed11923309
UniProtO69007

[Back to BioLiP]