Structure of PDB 4h8h Chain B

Receptor sequence
>4h8hB (length=553) Species: 1071045 (Rhizobium sp. MX-45) [Search protein sequence]
APWWKSAVFYQVYPRSFKDTNGDGIGDFKGLTEKLDYLKGLGIDAIWINP
HYASPNTDNGYDISDYREVMKEYGTMEDFDRLMAELKKRGMRLMVDVVIN
HSSDQHEWFKSSRASKDNPYRDYYFWRDGKDGHEPNNYPSFFGGSAWEKD
PVTGQYYLHYFGRQQPDLNWDTPKLREELYAMLRFWLDKGVSGMRFDTVA
TYSKTPGFPDLTPEQMKNFAEAYTQGPNLHRYLQEMHEKVFDHYDAVTAG
QIFGAPLNQVPLFIDSRRKELDMAFTFDLIRYDRALDRWHTIPRTLADFR
QTIDKVDAIAGEYGWNTFFLGNHDNPRAVSHFGDDRPQWREASAKALATV
TLTQRGTPFIFQGDELGMTNYPFKTLQDFDDIEVKGFFQDYVETGKATAE
ELLTNVALTSRNNARTPFQWDDSANAGFTTGKPWLKVNPNYTEINAAREI
GDPKSVYSFYRNLISIRHETPALSTGSYRDIDPSNADVYAYTRSQDGETY
LVVVNFKAEPRSFTLPDGMHIAETLIESSSPAAPAAGAASLELQPWQSGI
YKV
3D structure
PDB4h8h Insights into product binding in sucrose isomerases from crystal structures of MutB from Rhizobium sp.
ChainB
Resolution2.0 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 Q254 H326 D327
Catalytic site (residue number reindexed from 1) D96 R195 D197 Q251 H323 D324
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 D19 N21 D23 I25 D27
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:4h8h, PDBe:4h8h, PDBj:4h8h
PDBsum4h8h
PubMed
UniProtM1E1F6

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