Structure of PDB 3mmd Chain A

Receptor sequence
>3mmdA (length=371) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence]
KPHISALNAPQLDQRYKNEFTIGAAVEPYQLQNEKDVQMLKRHFNSIVAE
NVMKPISIQPEEGKFNFEQADRIVKFAKANGMDIRFHTLVWHSQVPQWFF
LDKEGKPMVNETDPVKREQNKQLLLKRLETHIKTIVERYKDDIKYWDVVN
EVVGDDGKLRNSPWYQIAGIDYIKVAFQAARKYGGDNIKLYMNDYNTEVE
PKRTALYNLVKQLKEEGVPIDGIGHQSHIQIGAPSEAEIEKTINMFAALG
LDNQITELDVSMYGWPPRAYPTYDAIPKQKFLDQAARYDRLFKLYEKLSD
KISNVTFWGIADNHTWLDSRADVYYDANGNVVVDPNAPYAKVEKGKGKDA
PFVFGPDYKVKPAYWAIIDHK
3D structure
PDB3mmd Structural-based rational mutagenesis of xylanases from G.stearothermophilus
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E159 N201 H236 E265 D267
Catalytic site (residue number reindexed from 1) E151 N193 H228 E257 D259
Enzyme Commision number 3.2.1.8: endo-1,4-beta-xylanase.
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 XYP A E159 W324 R328 E151 W316 R320
BS02 XYP A K62 H95 W99 E159 Q234 E265 W316 W324 K54 H87 W91 E151 Q226 E257 W308 W316
BS03 XYP A E58 N59 K62 Q102 W316 W324 E50 N51 K54 Q94 W308 W316
BS04 ZN A H11 D365 H3 D357
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0031176 endo-1,4-beta-xylanase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0045493 xylan catabolic process
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Cellular Component
External links
PDB RCSB:3mmd, PDBe:3mmd, PDBj:3mmd
PDBsum3mmd
PubMed
UniProtP40943|XYN1_GEOSE Endo-1,4-beta-xylanase

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