Structure of PDB 1ogo Chain X

Receptor sequence
>1ogoX (length=572) Species: 28574 (Talaromyces minioluteus) [Search protein sequence]
TTANTHCGADFCTWWHDSGEINTQTPVQPGNVRQSHKYSVQVSLAGTNNF
HDSFVYESIPRNGNGRIYAPTDPPNSNTLDSSVDDGISIEPSIGLNMAWS
QFEYSHDVDVKILATDGSSLGSPSDVVIRPVSISYAISQSDDGGIVIRVP
ADANGRKFSVEFKTDLYTFLSDGNEYVTSGGSVVGVEPTNALVIFASPFL
PSGMIPHMTPDNTQTMTPGPINNGDWGAKSILYFPPGVYWMNQDQSGNSG
KLGSNHIRLNSNTYWVYLAPGAYVKGAIEYFTKQNFYATGHGILSGENYV
YQANAGDNYIAVKSDSTSLRMWWHNNLGGGQTWYCVGPTINAPPFNTMDF
NGNSGISSQISDYKQVGAFFFQTDGPEIYPNSVVHDVFWHVNDDAIKIYY
SGASVSRATIWKCHNDPIIQMGWTSRDISGVTIDTLNVIHTRYIKSETVV
PSAIIGASPFYASGMSPDSRKSISMTVSNVVCEGLCPSLFRITPLQNYKN
FVVKNVAFPDGLQTNSIGTGESIIPAASGLTMGLAISAWTIGGQKVTMEN
FQANSLGQFNIDGSYWGEWQIS
3D structure
PDB1ogo Dextranase from Penicillium Minioluteum. Reaction Course, Crystal Structure, and Product Complex
ChainX
Resolution1.65 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D376 D395
Catalytic site (residue number reindexed from 1) D374 D393
Enzyme Commision number 3.2.1.11: dextranase.
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 BGC X K447 E449 K445 E447
BS02 GLC X K315 Q374 D395 D418 K313 Q372 D393 D416
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0033904 dextranase activity
Cellular Component
GO:0005576 extracellular region

View graph for
Molecular Function
View graph for
Cellular Component
External links
PDB RCSB:1ogo, PDBe:1ogo, PDBj:1ogo
PDBsum1ogo
PubMed12962629
UniProtP48845|DEXT_TALMI Dextranase (Gene Name=DEX)

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