Structure of PDB 3ogr Chain A

Receptor sequence
>3ogrA (length=986) Species: 51453 (Trichoderma reesei) [Search protein sequence]
AKGPLQNIVTWDEHSLFVHGERVVIFSGEVHPFRLPVPSLYLDVFHKIKA
LGFNTVSFYVDWALLEGKPGRFRADGIFSLEPFFEAATKAGIYLLARPGP
YINAEVSGGGFPGWLQRVKGKLRTDAPDYLHATDNYVAHIASIIAKAQIT
NGGPVILYQPENEYSGAAEGVLFPNKPYMQYVIDQARNAGIIVPLINNDA
FPGGTGAPGTGLGSVDIYGHDGYPLGFDCAHPSAWPDNGLPTTWRQDHLN
ISPSTPFSLVEFQGGAFDPFGGWGFEQCSALVNHEFERVFYKNNMAAGVT
IFNIYMTFGGTNWGNLGHPGGYTSYDYGASIREDRRIDREKYSELKLQGQ
FLKVSPGYITATPENATQGVYSDSQNIVITPLLAKESGDFFVVRHANYSS
TDTASYTVKLPTSAGDLTIPQLGGSLTLTGRDSKIHVTDYPVGKFTLLYS
TAEIFTWNEFAEKTVLVLYGGAQELHEFAVKNPFGSSKTAKAKKIEGSNV
TIHTTSNLTVVLQWTASSARQVVQLGSLVIYMVDRNSAYNYWVPTLPGSG
KQSAYGSSLMNPDSVIINGGYLIRSVAIKGNALSVQADFNVTTPLEIIGI
PKGISKLAVNGKELGYSVSELGDWIAHPAIEIPHVQVPELTKLKWYKVDS
LPEIRSNYDDSRWPLANLRTSNNTYAPLKTPVSLYGSDYGFHAGTLLFRG
RFTARTARQQLFLSTQGGSAFASSVWLNDRFIGSFTGFDAASAANSSYTL
DRLVRGRRYILTVVVDSTGLDENWTTGDDSMKAPRGILDYALTSSSGANV
SISWKLTGNLGGEDYRDVFRGPLNEGGLFFERQGFHLPSPPLSDFTHGPS
SSSSSSSPLDGIAHAGIAFYAAKLPLHLPAQEYDIPLSFVFDNATAAAPY
RALLYVNGFQYGKYVSNIGPQTEFPVPEGILDYNGDNWIGVALWALESRG
AKVPGLALKSKSPILTGRERVEVVKGPHFKKRHGAY
3D structure
PDB3ogr Crystal structures of Trichoderma reesei beta-galactosidase reveal conformational changes in the active site
ChainA
Resolution1.5 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.23: beta-galactosidase.
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 MAN A E377 N573 E340 N536
BS02 MAN A E322 R325 E285 R288
BS03 MAN A A317 N320 A280 N283
BS04 BMA A F775 D776 F738 D739
BS05 MAN A D265 W310 D228 W273
BS06 MAN A P306 D776 A777 P269 D739 A740
BS07 GLC A D265 F304 D228 F267
BS08 GAL A Y96 N140 A141 E142 E200 Y260 F264 E298 F304 Y342 Y364 Y59 N103 A104 E105 E163 Y223 F227 E261 F267 Y305 Y327
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004565 beta-galactosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0005975 carbohydrate metabolic process
Cellular Component
GO:0005773 vacuole

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3ogr, PDBe:3ogr, PDBj:3ogr
PDBsum3ogr
PubMed21130883
UniProtQ70SY0

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