Structure of PDB 1ur0 Chain A

Receptor sequence
>1ur0A (length=386) Species: 1402 (Bacillus licheniformis) [Search protein sequence]
GLYVEKVSGLRKDFIKGVDVSSIIALEESGVAFYNESGKKQDIFKTLKEA
GVNYVRVRIWNDPYDANGNGYGGGNNDLEKAIQIGKRATANGMKLLADFH
YSDFWADPAKQKAPKAWANLNFEDKKTALYQYTKQSLKAMKAAGIDIGMV
QVGNETNGGLAGETDWAKMSQLFNAGSQAVRETDSNILVALHFTNPETSG
RYAWIAETLHRHHVDYDVFASSYYPFWHGTLKNLTSVLTSVADTYGKKVM
VAETSYTYTAEDGDGHGNTAPKNGQTLNNPVTVQGQANAVRDVIQAVSDV
GEAGIGVFYWEPAWIPVGPAHRLEKNKALWETYGSGWATSYAAEYDPEDA
GKWFGGSAVDNQALFDFKGRPLPSLHVFQYVDTGTP
3D structure
PDB1ur0 The Structure of Endo-Beta-1,4-Galactanase from Bacillus Licheniformis in Complex with Two Oligosaccharide Products
ChainA
Resolution2.5 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) R66 E165 E263
Catalytic site (residue number reindexed from 1) R56 E155 E253
Enzyme Commision number 3.2.1.-
3.2.1.89: arabinogalactan endo-beta-1,4-galactanase.
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 GAL A W115 D117 W105 D107
BS02 GAL A W347 D359 W337 D349
BS03 GAL A H276 G277 K282 W363 H266 G267 K272 W353
BS04 CA A D272 D274 H276 N278 S367 D370 D262 D264 H266 N268 S357 D360
Gene Ontology
Molecular Function
GO:0015926 glucosidase activity

View graph for
Molecular Function
External links
PDB RCSB:1ur0, PDBe:1ur0, PDBj:1ur0
PDBsum1ur0
PubMed15312766
UniProtQ65CX5|GANB_BACLD Endo-beta-1,4-galactanase (Gene Name=ganB)

[Back to BioLiP]