Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3D5Y

High resolution crystal structure of 1,5-alpha-arabinanase catalytic mutant (AbnBE201A)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005737cellular_componentcytoplasm
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0031222biological_processarabinan catabolic process
A0046558molecular_functionarabinan endo-1,5-alpha-L-arabinosidase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 400
ChainResidue
AHIS271
AHOH1001
AHOH1006
AHOH1018
AHOH1019
AHOH1052
AHOH1151

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:19505290
ChainResidueDetails
AASP27

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:19505290
ChainResidueDetails
AALA201

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:19505290
ChainResidueDetails
AASP27
AGLY105
AASN144
ASER164

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
AHIS271

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Important for catalytic activity, responsible for pKa modulation of the active site Glu and correct orientation of both the proton donor and substrate => ECO:0000305|PubMed:19505290
ChainResidueDetails
AASP147

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Important for substrate recognition => ECO:0000250
ChainResidueDetails
AHIS271

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon