Structure of PDB 1yq2 Chain D

Receptor sequence
>1yq2D (length=1020) Species: 192168 (Arthrobacter sp. C2-2) [Search protein sequence]
ADVSYLTDQGPGSGRRVPARSWLHSDAPALSLNGDWRFRLLPAAPGTAGA
GSVLPSGETVEGVAAESYDDAAWDTLPVPSHWVMGQDGKYGRPIYTNVQY
PFPIDPPHVPDANPTGDFRRRFDVPAQWFESTTAALTLRFDGVESRYKVW
VNGQEIGVGSGSRLAQEFDVSDALRAGSNLLVVRVHQWSAASYLEDQDQW
WLPGIFRDVTLQARPAGGITDAWLRTGWSARSGAGTGTIDPEITADATAF
PVTLSVPELGVNVTWKSAEEVAPLALENVEPWSAEVPRLYEASVSSAAES
ISVRLGFRTVRIVGDQFLVNGRRVVFHGVNRHETHPDRGRVFDEAGARED
LALMKRFNVNAIRTSHYPPHPRLLDLADEMGFWVILECDLETHGFEAGGW
VENPSDVPAWRDALVDRMERTVERDKNHPSIVMWSLGNESGTGSNLAAMA
AWAHARDSSRPVHYEGDYTGAYTDVYSRMYSSIPETDSIGRNDSHALLLG
CDSAESARQRTKPFILCEYVHAMGNGPGAMDQYEALVDKYPRLHGGFVWE
WRDHGIRTRTAEGMEFFAYGGDFGEVVHDSNFVMDGMVLSDSTPTPGLYE
FKQIVSPIRLGLSLPAGGKPTLAVANLRHTADASDVVLRWRVEHDGAVAA
SGEVAAEGSDGPLRAGESATIALPAMPAAPLGETWLTVEAVLRDATGWAP
AGHPLGAVQLDLSAPAVPTRSPRPATPLDGALPVSLGPATFDAGTLVSLA
GQPVSGPRLELWRAPTDNDRGAGFGAYGPGDPWLNSGRGVPAPSSEAVWK
QAGLDRLTRRVEDVAALPDGIRVRTRYAAADSTHSVAVEENWQLDGGELC
LRIDITPSAGWNLVWPRIGVRWDLPTDVDGAAWFGAGPRESYPDSMHATM
VARHAASLEELNVPYARPQETGHRSDVRWLELDRAGAPWLRIDAEPDAAG
RRPGFSLARHTAQEIAAAGHPHELPTPSHSYLYVDAAQHGLGSRACGPDV
WPDFALRPEARTLKLRISPA
3D structure
PDB1yq2 Cold-active beta-Galactosidase from Arthrobacter sp. C2-2 Forms Compact 660kDa Hexamers: Crystal Structure at 1.9A Resolution
ChainD
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D201 H335 H369 E394 H396 E442 Y483 E521 H581 F585 D588
Catalytic site (residue number reindexed from 1) D198 H332 H366 E391 H393 E439 Y480 E518 H578 F582 D585
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 MG D A525 G527 G529 A522 G524 G526
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
GO:0046872 metal ion 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:1yq2, PDBe:1yq2, PDBj:1yq2
PDBsum1yq2
PubMed16171818
UniProtQ8KRF6

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