Structure of PDB 2ccr Chain A

Receptor sequence
>2ccrA (length=386) Species: 1402 (Bacillus licheniformis) [Search protein sequence]
GLYVEKVSGLRKDFIKGVDVSSIIALEESGVAFYNESGKKQDIFKTLKEA
GVNYVRVRIWNDPYDANGNGYGGGNNDLEKAIQIGKRATANGMKLLADFH
YSDFWADPAKQKAPKAWANLNFEDKKTALYQYTKQSLKAMKAAGIDIGMV
QVGNETNGGLAGETDWAKMSQLFNAGSQAVRETDSNILVALHFTNPETSG
RYAWIAETLHRHHVDYDVFASSYYPFWHGTLKNLTSVLTSVADTYGKKVM
VAETSYTYTAEDGDGHGNTAPKNGQTLNNPVTVQGQANAVRDVIQAVSDV
GEAGIGVFYWEPAWIPVGPAHRLEKNKALWETYGSGWATSYAAEYDPEDA
GKWFGGSAVDNQALFDFKGRPLPSLHVFQYVDTGTP
3D structure
PDB2ccr Investigating the Binding of Beta-1,4-Galactan to Bacillus Licheniformis Beta-1,4-Galactanase by Crystallography and Computational Modeling.
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 H276 W347 D359 H266 W337 D349
BS03 GAL A G277 K282 W363 G267 K272 W353
BS04 GAL A P118 N205 P108 N195
BS05 GAL A E165 T204 N205 H238 E155 T194 N195 H228
BS06 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:2ccr, PDBe:2ccr, PDBj:2ccr
PDBsum2ccr
PubMed19089956
UniProtQ65CX5|GANB_BACLD Endo-beta-1,4-galactanase (Gene Name=ganB)

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