Structure of PDB 4ha4 Chain A

Receptor sequence
>4ha4A (length=489) Species: 666510 (Acidilobus saccharovorans 345-15) [Search protein sequence]
AVTFPKDFLFGWSQAGFQSEMGTPGSEDPNSDWYAWVHDRENIAAGLVSG
DFPENGPGYWGNYRKFHDAAQAMGLTAARIGVEWSRIFPRPTFDVKVDAE
VKGDDVLSVYVSEGALEQLDKMANRDAINHYREMFSDLRSRGITFILNLY
HWPLPLWLHDPIAIRRGNLSAPSGWLDVRTVIEFAKFSAYVAWKLDDLVY
MYSTMNEPNVVWGLGYAAVKSGFPPGYLCLECAGRAMKNLVQAHARAYDA
VKAITKKPVGVIYANSDFTPLTDADREAAERAKFDNRWAFFDAVVRGQLG
GSTRDDLKGRLDWIGVNYYTRQVVRARGSGYEIVPGYGHGCEPNGVSPAG
RPCSDFGWEFYPEGLYNVLKEYWDRYHLPLLVTENGIADEGDYQRPYYLV
SHVYQVHRALQDGVNVIGYLHWSLADNYEWASGFSKRFGLLMVDYSTKRL
HWRPSAFIYREIAKSRAITDEIEHLNSVPPLRGLSPGHR
3D structure
PDB4ha4 Structures of beta-glycosidase from Acidilobus saccharovorans in complexes with tris and glycerol.
ChainA
Resolution1.37 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R80 H152 E208 V211 N318 Y320 E385
Catalytic site (residue number reindexed from 1) R79 H151 E207 V210 N317 Y319 E384
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 GOL A W153 F357 E430 W152 F356 E429
BS02 GOL A E391 R438 E390 R437
BS03 GOL A Q19 H152 N207 E208 E385 W423 E430 Q18 H151 N206 E207 E384 W422 E429
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004565 beta-galactosidase activity
GO:0008422 beta-glucosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4ha4, PDBe:4ha4, PDBj:4ha4
PDBsum4ha4
PubMed23657657
UniProtD9PZ08

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