Structure of PDB 3ob8 Chain A

Receptor sequence
>3ob8A (length=1024) Species: 28985 (Kluyveromyces lactis) [Search protein sequence]
SCLIPENLRNPKKVHENRLPTRAYYYDQDIFESLNGPWAFALFDAPLDAP
DAKNLDWETAKKWSTISVPSHWELQEDWKYGKPIYTNVQYPIPIDIPNPP
TVNPTGVYARTFELDSKSIESFEHRLRFEGVDNCYELYVNGQYVGFNKGS
RNGAEFDIQKYVSEGENLVVVKVFKWSDSTYIEDQDQWWLSGIYRDVSLL
KLPKKAHIEDVRVTTTFVDSQYQDAELSVKVDVQGSSYDHINFTLYEPED
GSKVYDASSLLNEENGNTTFSTKEFISFSTKKNEETAFKINVKAPEHWTA
ENPTLYKYQLDLIGSDGSVIQSIKHHVGFRQVELKDGNITVNGKDILFRG
VNRHDHHPRFGRAVPLDFVVRDLILMKKFNINAVRNSHYPNHPKVYDLFD
KLGFWVIDEADLETHGVQEPFNRHTNLEAEYPDTKNKLYDVNAHYLSDNP
EYEVAYLDRASQLVLRDVNHPSIIIWSLGNEACYGRNHKAMYKLIKQLDP
TRLVHYEGDLNALSADIFSFMYPTFEIMERWRKNHTDENGKFEKPLILCE
YGHAMGNGPGSLKEYQELFYKEKFYQGGFIWEWANHGIEFEDVSTADGKL
HKAYAYGGDFKEEVHDGVFIMDGLCNSEHNPTPGLVEYKKVIEPVHIKIA
HGSVTITNKHDFITTDHLLFIDKDTGKTIDVPSLKPEESVTIPSDTTYVV
AVLKDDAGVLKAGHEIAWGQAELPLKVPDFVTETAEKAAKINDGKRYVSV
ESSGLHFILDKLLGKIESLKVKGKEISSKFEGSSITFWRPPTNNDEPRDF
KNWKKYNIDLMKQNIHGVSVEKGSNGSLAVVTVNSRISPVVFYYGFETVQ
KYTIFANKINLNTSMKLTGEYQPPDFPRVGYEFWLGDSYESFEWLGRGPG
ESYPDKKESQRFGLYDSKDVEEFVYDYPQENGNHTDTHFLNIKFEGAGKL
SIFQKEKPFNFKISDEYGVDEAAHACDVKRYGRHYLRLDHAIHGVGSEAC
GPAVLDQYRLKAQDFNFEFDLAFE
3D structure
PDB3ob8 Structural basis of specificity in tetrameric Kluyveromyces lactis beta-galactosidase.
ChainA
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D187 H355 H389 E414 H416 E482 Y523 E551 H616 F620 D623
Catalytic site (residue number reindexed from 1) D186 H354 H388 E413 H415 E481 Y522 E550 H615 F619 D622
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 GAL A D187 H389 N481 E482 M522 E551 H554 W582 D186 H388 N480 E481 M521 E550 H553 W581
BS02 MG A E414 H416 E482 E413 H415 E481
BS03 MN A D593 H975 D978 D592 H974 D977
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004565 beta-galactosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0030246 carbohydrate binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0005990 lactose catabolic process
GO:0009056 catabolic process
Cellular Component
GO:0009341 beta-galactosidase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3ob8, PDBe:3ob8, PDBj:3ob8
PDBsum3ob8
PubMed22193516
UniProtP00723|BGAL_KLULA Beta-galactosidase (Gene Name=LAC4)

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