1WAU
Structure of KDPG Aldolase E45N mutant
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 | (R,S)-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 | 0016832 | molecular_function | aldehyde-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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A1214 |
| Chain | Residue |
| A | GLY162 |
| A | GLY163 |
| A | ILE164 |
| A | SER184 |
| A | HOH2098 |
| A | HOH2100 |
| A | HOH2101 |
| A | HOH2102 |
Functional Information from PROSITE/UniProt
| site_id | PS00160 |
| Number of Residues | 14 |
| Details | ALDOLASE_KDPG_KHG_2 KDPG and KHG aldolases Schiff-base forming residue. GlkeFKFFPAeanG |
| Chain | Residue | Details |
| A | GLY128-GLY141 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"11274385","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"11342129","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16403639","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"1978721","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Schiff-base intermediate with substrate","evidences":[{"source":"PubMed","id":"11274385","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11342129","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16403639","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"3136164","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11274385","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EUA","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"11274385","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EUA","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Site: {"description":"Plays a major role in determining the stereoselectivity","evidences":[{"source":"PubMed","id":"17981470","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1fq0 |
| Chain | Residue | Details |
| A | LYS133 | |
| A | ASN45 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 550 |
| Chain | Residue | Details |
| A | ASN45 | proton acceptor, proton donor |
| A | ARG49 | electrostatic stabiliser, modifies pKa |
| A | LYS133 | electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor |
