Structure of PDB 4gi6 Chain A

Receptor sequence
>4gi6A (length=556) Species: 1071045 (Rhizobium sp. MX-45) [Search protein sequence]
PGAPWWKSAVFYQVYPRSFKDTNGDGIGDFKGLTEKLDYLKGLGIDAIWI
NPHYASPNTDNGYDISDYREVMKEYGTMEDFDRLMAELKKRGMRLMVDVV
INHSSDQHEWFKSSRASKDNPYRDYYFWRDGKDGHEPNNYPSFFGGSAWE
KDPVTGQYYLHYLGRQQPDLNWDTPKLREELYAMLRFWLDKGVSGMRFDT
VATYSKTPGFPDLTPEQMKNFAEAYTQGPNLHRYLQEMHEKVFDHYDAVT
AGEIFGAPLNQVPLFIDSRRKELDMAFTFDLIRYDRALDRWHTIPRTLAD
FRQTIDKVDAIAGEYGWNTFFLGNHDNPRAVSHFGDDRPQWREASAKALA
TVTLTQRGTPFIFQGDELGMTNYPFKTLQDFDDIEVKGFFQDYVETGKAT
AEELLTNVALTSRDNARTPFQWDDSANAGFTTGKPWLKVNPNYTEINAAR
EIGDPKSVYSFYRNLISIRHETPALSTGSYRDIDPSNADVYAYTRSQDGE
TYLVVVNFKAEPRSFTLPDGMHIAETLIESSSPAAPAAGAASLELQPWQS
GIYKVK
3D structure
PDB4gi6 Mutations inducing an active-site aperture in Rhizobium sp. sucrose isomerase confer hydrolytic activity
ChainA
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) D98 R197 D199 E253 H325 D326
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 A D22 N24 D26 I28 D30 D21 N23 D25 I27 D29
BS02 GLC A F144 E254 F256 D327 E386 F143 E253 F255 D326 E385
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
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Biological Process
External links
PDB RCSB:4gi6, PDBe:4gi6, PDBj:4gi6
PDBsum4gi6
PubMed23385465
UniProtM1E1F3

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