Structure of PDB 5e9a Chain C

Receptor sequence
>5e9aC (length=684) Species: 1591056 (Rahnella sp. R3) [Search protein sequence]
TKFPLLSSKISGLLHGADYNPEQWLDHPDVLVRDVEMMKEARCNVMSVGI
FSWSALEPEEGRYTFDWMDQVLNRLHENGISVFLATPSGARPAWMSQKYP
QVLRVGRDRVPALHGGRHNHCMSSPVYREKVQLMNGQLAKRYAHHPAVIG
WHISNEYGGECHCDTCQGQFRDWLKARYVTLDALNKAWWSTFWSHTYTDW
SQLESPSPQGENGVHGLNLDWRRFNTDQVTRFCSEEIRPLKAENPALPAT
TNFMEYFNDYDYWKLAGVLDFISWDSYPMWHTRQDDIGLAAYTAMYHDLM
RTLKQGKPFVLMESTPSFTNWQPTSKLKKPGMHILSSLQAVAHGADSVQY
FQWRKSRGSCEKFHGAVVDHVGHIDTRVGREVAELGSILSALAPVAGSRV
EAKVAIIFDWESRWAMDDAMGPRNAGLHYENTVADHYRALWAQGIAVDVI
NADCDLQGYDLVIAPMLYMVREGVGERISAFVQAGGRFVATYWSGIVNET
DLCFLNGFPGPLRPVLGIWAEEIDSLTDEQHNSVAGVEGNALGLSGPYRA
SQLCEVIHLEGAAALATYGDDFYAGNPAVTVNLYGKGQAYYVASRNDQQF
HADFFTALAKEMKLPRAINTPLPEGVTAARRTDGESEFIFLQNYNADNQT
VALPQDYQDIVHGGNLPRKLTLPAFGCQILTRKI
3D structure
PDB5e9a Cloning, expression and structural stability of a cold-adapted beta-galactosidase from Rahnella sp. R3.
ChainC
Resolution2.561 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 ZN C C122 C162 C164 C167 C121 C161 C163 C166
Gene Ontology
Molecular Function
GO:0004565 beta-galactosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006012 galactose metabolic 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:5e9a, PDBe:5e9a, PDBj:5e9a
PDBsum5e9a
PubMed26145832
UniProtA0A0B4U8I5

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