3LBC
D-sialic acid aldolase complexed with L-arabinose
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0008747 | molecular_function | N-acetylneuraminate lyase activity |
A | 0016829 | molecular_function | lyase activity |
A | 0019262 | biological_process | N-acetylneuraminate catabolic process |
A | 0042802 | molecular_function | identical protein binding |
A | 0044010 | biological_process | single-species biofilm formation |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0008747 | molecular_function | N-acetylneuraminate lyase activity |
B | 0016829 | molecular_function | lyase activity |
B | 0019262 | biological_process | N-acetylneuraminate catabolic process |
B | 0042802 | molecular_function | identical protein binding |
B | 0044010 | biological_process | single-species biofilm formation |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0005975 | biological_process | carbohydrate metabolic process |
C | 0008747 | molecular_function | N-acetylneuraminate lyase activity |
C | 0016829 | molecular_function | lyase activity |
C | 0019262 | biological_process | N-acetylneuraminate catabolic process |
C | 0042802 | molecular_function | identical protein binding |
C | 0044010 | biological_process | single-species biofilm formation |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0005975 | biological_process | carbohydrate metabolic process |
D | 0008747 | molecular_function | N-acetylneuraminate lyase activity |
D | 0016829 | molecular_function | lyase activity |
D | 0019262 | biological_process | N-acetylneuraminate catabolic process |
D | 0042802 | molecular_function | identical protein binding |
D | 0044010 | biological_process | single-species biofilm formation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE LAI A 1550 |
Chain | Residue |
A | GLY169 |
A | GLU192 |
A | HOH538 |
A | HOH551 |
A | HOH1515 |
A | SO41561 |
C | TYR172 |
C | HOH384 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 A 1554 |
Chain | Residue |
A | TYR43 |
A | GLY46 |
A | SER47 |
A | THR48 |
A | TYR137 |
A | LYS165 |
A | HOH327 |
A | ALA11 |
site_id | AC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SO4 A 1561 |
Chain | Residue |
A | PRO140 |
A | SER168 |
A | GLY169 |
A | TYR190 |
A | HOH662 |
A | HOH1086 |
A | HOH1285 |
A | HOH1489 |
A | HOH1515 |
A | LAI1550 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE LAI B 1551 |
Chain | Residue |
B | GLY169 |
B | GLU192 |
B | HOH472 |
B | HOH1517 |
B | SO41558 |
D | ASP170 |
D | TYR172 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 B 1556 |
Chain | Residue |
B | ALA11 |
B | TYR43 |
B | GLY46 |
B | SER47 |
B | THR48 |
B | TYR137 |
B | LYS165 |
B | HOH1131 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 B 1558 |
Chain | Residue |
B | PRO140 |
B | SER168 |
B | GLY169 |
B | TYR190 |
B | HOH729 |
B | HOH1026 |
B | HOH1485 |
B | LAI1551 |
site_id | AC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE LAI C 1552 |
Chain | Residue |
A | ASP170 |
A | TYR172 |
A | HOH426 |
C | GLY169 |
C | GLU192 |
C | HOH344 |
C | HOH669 |
C | HOH1506 |
C | SO41560 |
site_id | AC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 C 1557 |
Chain | Residue |
C | ALA11 |
C | TYR43 |
C | GLY46 |
C | SER47 |
C | THR48 |
C | TYR137 |
C | LYS165 |
C | HOH1099 |
C | HOH1510 |
site_id | AC9 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 C 1560 |
Chain | Residue |
C | SER168 |
C | GLY169 |
C | TYR190 |
C | HOH455 |
C | HOH991 |
C | HOH992 |
C | HOH1490 |
C | LAI1552 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE LAI D 1553 |
Chain | Residue |
D | GLY169 |
D | GLU192 |
D | HOH731 |
D | HOH1389 |
D | HOH1509 |
D | SO41559 |
site_id | BC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 D 1555 |
Chain | Residue |
D | ALA11 |
D | TYR43 |
D | GLY46 |
D | SER47 |
D | THR48 |
D | TYR137 |
D | LYS165 |
D | HOH325 |
D | HOH1366 |
site_id | BC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 D 1559 |
Chain | Residue |
D | SER168 |
D | GLY169 |
D | HOH466 |
D | HOH735 |
D | HOH1486 |
D | HOH1497 |
D | HOH1508 |
D | HOH1518 |
D | LAI1553 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:24521460 |
Chain | Residue | Details |
A | TYR137 | |
B | TYR137 | |
C | TYR137 | |
D | TYR137 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Schiff-base intermediate with substrate => ECO:0000269|PubMed:12711733, ECO:0000269|PubMed:19923724, ECO:0000269|PubMed:24521460, ECO:0000269|PubMed:9047371, ECO:0000305|PubMed:8081752 |
Chain | Residue | Details |
A | LYS165 | |
B | LYS165 | |
C | LYS165 | |
D | LYS165 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:9047371, ECO:0000305|PubMed:12711733, ECO:0007744|PDB:1FDY, ECO:0007744|PDB:1FDZ, ECO:0007744|PDB:1HL2 |
Chain | Residue | Details |
A | SER47 | |
A | THR48 | |
B | SER47 | |
B | THR48 | |
C | SER47 | |
C | THR48 | |
D | SER47 | |
D | THR48 |
site_id | SWS_FT_FI4 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL |
Chain | Residue | Details |
A | THR167 | |
B | SER208 | |
C | THR167 | |
C | GLY189 | |
C | ASP191 | |
C | GLU192 | |
C | SER208 | |
D | THR167 | |
D | GLY189 | |
D | ASP191 | |
D | GLU192 | |
A | GLY189 | |
D | SER208 | |
A | ASP191 | |
A | GLU192 | |
A | SER208 | |
B | THR167 | |
B | GLY189 | |
B | ASP191 | |
B | GLU192 |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | SITE: Required to correctly position the proton donor => ECO:0000305|PubMed:24521460 |
Chain | Residue | Details |
A | SER47 | |
A | TYR110 | |
B | SER47 | |
B | TYR110 | |
C | SER47 | |
C | TYR110 | |
D | SER47 | |
D | TYR110 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 2 |
Details | M-CSA 553 |
Chain | Residue | Details |
A | TYR137 | proton acceptor, proton donor, proton relay |
A | LYS165 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor |
site_id | MCSA2 |
Number of Residues | 2 |
Details | M-CSA 553 |
Chain | Residue | Details |
B | TYR137 | proton acceptor, proton donor, proton relay |
B | LYS165 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor |
site_id | MCSA3 |
Number of Residues | 2 |
Details | M-CSA 553 |
Chain | Residue | Details |
C | TYR137 | proton acceptor, proton donor, proton relay |
C | LYS165 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor |
site_id | MCSA4 |
Number of Residues | 2 |
Details | M-CSA 553 |
Chain | Residue | Details |
D | TYR137 | proton acceptor, proton donor, proton relay |
D | LYS165 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor |