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

4FLO

Crystal structure of Amylosucrase double mutant A289P-F290C from Neisseria polysaccharea

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0016757molecular_functionglycosyltransferase activity
A0047669molecular_functionamylosucrase activity
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE TRS A 701
ChainResidue
AASP144
AHOH814
ATYR147
AHIS187
APHE229
APHE250
AASP286
AGLU328
AARG509
AHOH800

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 702
ChainResidue
ATYR375
AARG376
AASP403
AHOH1273

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 703
ChainResidue
APRO203
AASP526
AHOH1254
AHOH1334

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 704
ChainResidue
AARG226
APHE250
ACYS290
AGLU300
AGLU328
AILE330

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE P6G A 705
ChainResidue
ALEU204
APHE205
ATRP263
AARG266
AALA267
AHOH916
AHOH1262

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:15023061, ECO:0000305|PubMed:10828446
ChainResidueDetails
AASP286

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:10828446
ChainResidueDetails
AGLU328

site_idSWS_FT_FI3
Number of Residues7
DetailsBINDING: BINDING => ECO:0000305|PubMed:11467966, ECO:0000305|PubMed:12364331, ECO:0000305|PubMed:15023061
ChainResidueDetails
AASP144
AHIS187
AGLN254
AARG284
AHIS392
AASP393
AARG509

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000250
ChainResidueDetails
AASP444

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon