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4FLR

Crystal structure of Amylosucrase double mutant A289P-F290L 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
AHOH875
ATYR147
AHIS187
APHE250
AASP286
AGLU328
AARG509
AGOL708
AGOL717

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GOL A 702
ChainResidue
AASP403

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 703
ChainResidue
AHIS332
APHE399
AASP401
AGLU402
AARG415

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 704
ChainResidue
AGLU328
AILE330
ATYR349
ATYR388
ASER391
AHIS392
AASP393
AGOL717
AHOH1000

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 705
ChainResidue
AARG86
AGLU87
APRO90
AARG317
APRO321
APHE324
AGOL706
AHOH835
AHOH921
AHOH922

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 706
ChainResidue
APRO90
AARG317
APHE324
AGLN342
AGLN346
AHIS382
AGOL705

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 707
ChainResidue
AASP91
ALEU94
ASER95
AASP552
AGLY553
AHOH964

site_idAC8
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GOL A 708
ChainResidue
ATYR104
AMET133
AASP144
AGLY145
ATYR147
AHIS392
AASP393
AARG509
AARG513
ATRS701
AHOH875
AHOH1004

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 709
ChainResidue
AGLY396
ATRP397
ATHR398
AASP444
ACYS445
AARG446

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 710
ChainResidue
AARG226
AILE228
AGLU328
AALA329
AILE330
AGOL717

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 711
ChainResidue
APHE229
AGLN232
AASN251
AGLN437
AASP506
AASP507
AARG509

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 712
ChainResidue
ATYR51
AASN54
ASER260
AASN562
ATHR589
ATHR592

site_idBC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 713
ChainResidue
AILE93
ALEU94
ASER95
AGLY480
ALEU481
AARG545
APHE551
AGLY553

site_idBC5
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL A 714
ChainResidue
ALYS564
AILE566
AHOH993
AHOH994
AHOH1012
AGLU55
AVAL366
APHE559
AASN560
ATHR561
AASN563

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 715
ChainResidue
AASN424
APHE426
AASP427
AGLY428
ASER429
AHOH1035

site_idBC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 716
ChainResidue
AASN207
AASN258
ASER260
AHIS591
AGLN594

site_idBC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 717
ChainResidue
APHE229
AGLU328
AASP393
AASP394
APHE436
AARG446
ATRS701
AGOL704
AGOL710

site_idBC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 718
ChainResidue
ATRP194
AGLU271
A1PE720

site_idCC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 719
ChainResidue
AASP202
APRO203
AASP526

site_idCC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 1PE A 720
ChainResidue
ALEU204
APHE205
APHE208
ATRP263
AARG266
AALA267
AGOL718
AHOH879
AHOH1013

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

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PDB entries from 2024-11-06

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