Structure of PDB 5x3j Chain A

Receptor sequence
>5x3jA (length=718) Species: 479435 (Kribbella flavida DSM 17836) [Search protein sequence]
MIKHRPHGIEHPYAVSPDQRVPVLPLAGEPVLLGVVAPEADRVVCEWGTL
ELPLSATSAAAADAAALAGGEGHLSEAQADGAWSVQTPPLAEPVKYRFHA
HRGGAAESTEWFEVSPAVWTADGVGEVRGGGERVRGVEWLVSSQGVHRGR
FRLQLQDGDRLVGFGERYDALDQRGRELDAVVFEQYKAQGVHGRTYLPMP
FAHVVGADGNGWGFHVRTSRRTWYSSAGNELTVEVALGDEPVVDLAIYEG
DPATVLTGFLDEVGRAEELPGWVFRLWASGNEWNTQQLVTARMDTHRDLA
IPVGAVVIEAWSDEQGITIWRDAVYAVTEDGSAHRAEDFSYRPDGAWPDP
KAMIDELHARGIKVILWQIPLQKTEFSTGQVAADAAAMVRDGHAVLEADG
TAYRNRGWWFPQALMPDLSVQRTRDWWTEKRRYLVEHFDVDGFKTAGGEH
AWGHDLVYADGRKGDEGNNLYPVHYARAFGDLLRSAGKAPVTFSRAGFTG
SQAHGIFWAGDEDSTWQAFRSSVTAGLTAASCGIVYWGWDLAGFSGPVPD
AELYLRAAAASAFMPIMQYHSEFNHHQLPLRDRTPWHVAETTGDDRVVPL
FRRFATLRESLVPYLTEQAARTIATDRPLMRPLFFDHENDPEIWNHPYQY
LLGDELLINPVLEPGATTWTTYLPAGEWIDVWTGDRVPSGLVTRDVPLEV
VPVYCRASRWSELQPVFS
3D structure
PDB5x3j Glycoside hydrolase mutant in complex with substrate
ChainA
Resolution2.3 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.204: 1,3-alpha-isomaltosidase.
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 GLC A H73 E189 Y191 W413 W414 R500 D516 E577 H73 E184 Y186 W408 W409 R495 D511 E572
BS02 GLC A E314 W414 R500 W513 D516 F549 H575 E309 W409 R495 W508 D511 F544 H570
BS03 GLC A N286 E319 W372 F578 N281 E314 W367 F573
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0030246 carbohydrate binding
Biological Process
GO:0000272 polysaccharide catabolic process
GO:0005975 carbohydrate metabolic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:5x3j, PDBe:5x3j, PDBj:5x3j
PDBsum5x3j
PubMed
UniProtD2PPM7|AIMA_KRIFD 1,3-alpha-isomaltosidase (Gene Name=Kfla_1895)

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