Structure of PDB 4gi9 Chain B

Receptor sequence
>4gi9B (length=555) Species: 1071045 (Rhizobium sp. MX-45) [Search protein sequence]
GAPWWKSAVFYQVYPRSFKDTNGDGIGDFKGLTEKLDYLKGLGIDAIWIN
PHYASPNTDNGYDISDYREVMKEYGTMEDFDRLMAELKKRGMRLMVDVVI
NHSSDQHEWFKSSRASKDNPYRDYYFWRDGKDGHEPNNYPSFFGGSAWEK
DPVTGQYYLHYLGRQQPDLNWDTPKLREELYAMLRFWLDKGVSGMRFDTV
ATYSKTPGFPDLTPEQMKNFAEAYTQGPNLHRYLQEMHEKVFDHYDAVTA
GEIFGAPLNQVPLFIDSRRKELDMAFTFDLIRYDRALDRWHTIPRTLADF
RQTIDKVDAIAGEYGWNTFFLGNHDNPRAVSHFGDDRPQWREASAKALAT
VTLTQRGTPFIFQGDELGMTNYPFKTLQDFDDIEVKGFFQDYVETGKATA
EELLTNVALTSRDNARTPFQWDDSANAGFTTGKPWLKVNPNYTEINAARE
IGDPKSVYSFYRNLISIRHETPALSTGSYRDIDPSNADVYAYTRSQDGET
YLVVVNFKAEPRSFTLPDGMHIAETLIESSSPAAPAAGAASLELQPWQSG
IYKVK
3D structure
PDB4gi9 Mutations inducing an active-site aperture in Rhizobium sp. sucrose isomerase confer hydrolytic activity
ChainB
Resolution2.15 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D99 R198 D200 E254 H326 D327
Catalytic site (residue number reindexed from 1) D97 R196 D198 E252 H324 D325
Enzyme Commision number 5.4.11.99
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 CA B D22 N24 D26 I28 D30 D20 N22 D24 I26 D28
Gene Ontology
Molecular Function
GO:0004556 alpha-amylase activity
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0009313 oligosaccharide catabolic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4gi9, PDBe:4gi9, PDBj:4gi9
PDBsum4gi9
PubMed23385465
UniProtM1E1F3

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