Structure of PDB 4re4 Chain A

Receptor sequence
>4re4A (length=483) Species: 39946 (Oryza sativa Indica Group) [Search protein sequence]
AAPFTYWLNPEIYDAGGLSRRAFPEGFVFGTAASAYQVEGMAKQGGRGPS
IWDAFIEKPGTIPNNATADVTVDEYHRYKEDVNIMKNMGFDAYRFSISWS
RIFPNGTGMVNQEGVDYYNRLIDYMVKKGIKPYANLYHYDLPLALHEQYL
GWLSPNIVEAFADYADFCFQTFGDRVKDWFTFNEPRCVAALGYDNGFHAP
GRCSGCDAGGNSTTEPYLAAHHLILSHAAAVKRYREKYQLYQKGRIGILL
DFVWYEPFSDSNADRAAAQRARDFHLGWFLDPIIHGRYPYSMLEIVKDRM
PTFSDEESRMVKDSIDYVGINHYTSFYMKDPGPWNLTPTSYQDDWHVGFA
YERNGVPIGAQANSYWLYIVPWGINKAVTYVKETYGNPTMILSENGMDQP
GNVSITQGVHDTVRIRYYRNYITELKKAIDDGAKVIGYFAWSLLDNFEWR
LGYTSRFGIVYVDYKTLKRYPKDSAFWFKNMLS
3D structure
PDB4re4 A Single Glycosidase Harnesses Different Pyranoside Ring Transition State Conformations for Hydrolysis of Mannosides and Glucosides
ChainA
Resolution2.29 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R89 H133 E179 C182 N316 Y318 E389
Catalytic site (residue number reindexed from 1) R94 H138 E184 C187 N321 Y323 E394
Enzyme Commision number 3.2.1.25: beta-mannosidase.
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 IFM A Q32 H133 E179 Y318 E389 W436 E443 W444 F452 Q37 H138 E184 Y323 E394 W441 E448 W449 F457 PDBbind-CN: -logKd/Ki=6.87,Ki=135nM
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004565 beta-galactosidase activity
GO:0008422 beta-glucosidase activity
GO:0033907 beta-D-fucosidase activity
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function

View graph for
Biological Process
External links
PDB RCSB:4re4, PDBe:4re4, PDBj:4re4
PDBsum4re4
PubMed
UniProtA2YPH1

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