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

1QI4

MUTANT (E219G) MALTOTETRAOSE-FORMING EXO-AMYLASE IN COMPLEX WITH MALTOTETRAOSE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004556molecular_functionalpha-amylase activity
A0005975biological_processcarbohydrate metabolic process
A0043169molecular_functioncation binding
Functional Information from PDB Data
site_idNUL
Number of Residues3
Details
ChainResidue
AASP193
AGLY219
AASP294

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:10556241
ChainResidueDetails
AASP193

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:10556241, ECO:0000305|PubMed:9281429
ChainResidueDetails
AGLY219

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:10556241, ECO:0000269|PubMed:9126844, ECO:0000269|PubMed:9281429
ChainResidueDetails
AASP1
AGLU17
AASN116
AASP151
AASP154
AASP162
AGLY197
AGLN2
AHIS13
AASP16

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:10556241
ChainResidueDetails
APHE156
AGLN305
ATYR78

site_idSWS_FT_FI5
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:10556241, ECO:0000305|PubMed:9281429
ChainResidueDetails
AHIS117
AARG191
AHIS293

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P0C1B3
ChainResidueDetails
AARG196

site_idSWS_FT_FI7
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000305|PubMed:10556241
ChainResidueDetails
AASP294

218500

PDB entries from 2024-04-17

PDB statisticsPDBj update infoContact PDBjnumon