1FQ0
KDPG ALDOLASE FROM ESCHERICHIA COLI
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0008675 | molecular_function | 2-dehydro-3-deoxy-phosphogluconate aldolase activity |
A | 0008700 | molecular_function | 4-hydroxy-2-oxoglutarate aldolase activity |
A | 0008948 | molecular_function | oxaloacetate decarboxylase activity |
A | 0009255 | biological_process | Entner-Doudoroff pathway through 6-phosphogluconate |
A | 0016020 | cellular_component | membrane |
A | 0016829 | molecular_function | lyase activity |
A | 0016833 | molecular_function | oxo-acid-lyase activity |
A | 0042802 | molecular_function | identical protein binding |
A | 0106009 | molecular_function | (4S)-4-hydroxy-2-oxoglutarate aldolase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0008675 | molecular_function | 2-dehydro-3-deoxy-phosphogluconate aldolase activity |
B | 0008700 | molecular_function | 4-hydroxy-2-oxoglutarate aldolase activity |
B | 0008948 | molecular_function | oxaloacetate decarboxylase activity |
B | 0009255 | biological_process | Entner-Doudoroff pathway through 6-phosphogluconate |
B | 0016020 | cellular_component | membrane |
B | 0016829 | molecular_function | lyase activity |
B | 0016833 | molecular_function | oxo-acid-lyase activity |
B | 0042802 | molecular_function | identical protein binding |
B | 0106009 | molecular_function | (4S)-4-hydroxy-2-oxoglutarate aldolase activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0008675 | molecular_function | 2-dehydro-3-deoxy-phosphogluconate aldolase activity |
C | 0008700 | molecular_function | 4-hydroxy-2-oxoglutarate aldolase activity |
C | 0008948 | molecular_function | oxaloacetate decarboxylase activity |
C | 0009255 | biological_process | Entner-Doudoroff pathway through 6-phosphogluconate |
C | 0016020 | cellular_component | membrane |
C | 0016829 | molecular_function | lyase activity |
C | 0016833 | molecular_function | oxo-acid-lyase activity |
C | 0042802 | molecular_function | identical protein binding |
C | 0106009 | molecular_function | (4S)-4-hydroxy-2-oxoglutarate aldolase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE CIT A 509 |
Chain | Residue |
A | VAL20 |
A | HOH575 |
C | PRO152 |
A | GLU45 |
A | THR47 |
A | ARG49 |
A | GLY72 |
A | THR73 |
A | LYS133 |
A | PHE135 |
A | THR161 |
site_id | AC2 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE CIT B 510 |
Chain | Residue |
A | PRO152 |
B | VAL20 |
B | GLU45 |
B | THR47 |
B | ARG49 |
B | GLY72 |
B | THR73 |
B | ILE92 |
B | PRO94 |
B | LYS133 |
B | PHE135 |
B | THR161 |
site_id | AC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE CIT C 511 |
Chain | Residue |
B | PRO152 |
C | VAL20 |
C | GLU45 |
C | THR47 |
C | ARG49 |
C | GLY72 |
C | THR73 |
C | PRO94 |
C | LYS133 |
C | PHE135 |
C | THR161 |
C | HOH651 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | GLU45 | |
B | GLU45 | |
C | GLU45 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | ACT_SITE: |
Chain | Residue | Details |
A | ARG49 | |
B | ARG49 | |
C | ARG49 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | ACT_SITE: Schiff-base intermediate with substrate |
Chain | Residue | Details |
A | LYS133 | |
B | LYS133 | |
C | LYS133 |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | BINDING: |
Chain | Residue | Details |
A | ALA8 | |
B | ALA8 | |
C | ALA8 |
site_id | SWS_FT_FI5 |
Number of Residues | 15 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16403639 |
Chain | Residue | Details |
A | ARG49 | |
B | SER184 | |
C | ARG49 | |
C | THR73 | |
C | THR161 | |
C | GLY163 | |
C | SER184 | |
A | THR73 | |
A | THR161 | |
A | GLY163 | |
A | SER184 | |
B | ARG49 | |
B | THR73 | |
B | THR161 | |
B | GLY163 |
site_id | SWS_FT_FI6 |
Number of Residues | 3 |
Details | BINDING: covalent => ECO:0000269|PubMed:16403639 |
Chain | Residue | Details |
A | LYS133 | |
B | LYS133 | |
C | LYS133 |
site_id | SWS_FT_FI7 |
Number of Residues | 3 |
Details | SITE: Plays a major role in determining the stereoselectivity |
Chain | Residue | Details |
A | THR161 | |
B | THR161 | |
C | THR161 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | a catalytic site defined by CSA, PubMed 16403639 |
Chain | Residue | Details |
A | GLU45 | |
A | LYS133 | |
A | ARG49 |
site_id | MCSA1 |
Number of Residues | 3 |
Details | M-CSA 550 |
Chain | Residue | Details |
A | GLU45 | proton acceptor, proton donor |
A | ARG49 | electrostatic stabiliser, modifies pKa |
A | LYS133 | electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor |
site_id | MCSA2 |
Number of Residues | 3 |
Details | M-CSA 550 |
Chain | Residue | Details |
B | GLU45 | proton acceptor, proton donor |
B | ARG49 | electrostatic stabiliser, modifies pKa |
B | LYS133 | electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor |
site_id | MCSA3 |
Number of Residues | 3 |
Details | M-CSA 550 |
Chain | Residue | Details |
C | GLU45 | proton acceptor, proton donor |
C | ARG49 | electrostatic stabiliser, modifies pKa |
C | LYS133 | electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor |