Structure of PDB 5ldr Chain A

Receptor sequence

>5ldrA (length=731) Species: 687527 (Paracoccus sp. 32d)

MRVTQKLNHGWIFAEGAADPATPLAGETVTLPHNAVDLPLSYFDETSYQR
AFTYQRVIAWDDAWQGRRVQLRFDGAMADNVVWVNGVQVVAHPDGYTPFV
ADLTDHLRPGDNLVTVRIDGSENPAIPPFGAQIDYLTYAGIYRDVWLMVL
PERHLTNARILTPDALSDAKTVVIRPEVTAPGPVRARLLDGDREIAATEG
EGELTLAGLTGLSLWSTDNPQLYTVELTLPDSGDVTTHRFGFRTAEWTPQ
GFLLNGQPMKLRGLNRHQSWAHQGYAAGRHAQERDAEIVRHDLCCNMVRT
SHYPQSTWFLDRCDEIGLLVFEEIPGWQHIGDQAWQDRSVDNVRAMITRD
WNHPSIVIWGVRINESPDNHDFYVRTNALARELDPTRAIGGVRCITDSEM
LEDVYTMNDFILDESELPLINRPRTALRPTEEVTGIKKPVPYLVTEYNGH
MFPTKAQDPELRQMEHVIRHLEVLNAAHGDPAISGCIGWCMFDYNTHKDF
GAGDRICHHGVMDIWREPKFAAHAYGSQKPPSEGIVMEPVTFWARGERNI
GGVLPLIVLTNCDEVEFECAGVTRRVGPDRERFPHLPRPPVIIDHRHISA
EELGQWGMSWHPGRITGWLNGEQVALREYVADPLPTTLQIAPDRDTLPAD
GDIDLRVMLRALDQVGNRLPFLDAGIAVTVDGPARLIGPDLRMLQGGTTG
MLLRLTGDAGTIRITARHPQFPEAVATVTVG

3D structure

• PDB: 5ldr Structural studies of a cold-adapted dimeric beta-D-galactosidase from Paracoccus sp. 32d.
• Chain: A
• Resolution: 3.15 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D134 H267 H302 W327 H329 E365 F410 E446 A502 I506 H509
• Catalytic site (residue number reindexed from 1): D134 H267 H302 W327 H329 E365 F410 E446 A502 I506 H509
• 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	D134 H302 W327 N364 E365 E446 H450 W489	D134 H302 W327 N364 E365 E446 H450 W489
BS02	GLC	A	P612 G613 R614	P612 G613 R614

Gene Ontology

Molecular Function

• GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
• GO:0016798 hydrolase activity, acting on glycosyl bonds

Biological Process

• GO:0005975 carbohydrate metabolic process

External links

• PDB: RCSB:5ldr, PDBe:5ldr, PDBj:5ldr
• PDBsum: 5ldr
• PubMed: 27599737
• UniProt: D1LZK0