1MXS
Crystal structure of 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase from Pseudomonas putida.
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 299 |
| Chain | Residue |
| A | GLY174 |
| A | GLY175 |
| A | THR195 |
| A | THR196 |
| A | HOH305 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 300 |
| Chain | Residue |
| A | VAL104 |
| A | THR105 |
| A | PRO106 |
| A | LYS145 |
| A | GLU57 |
| A | ARG61 |
| A | GLY84 |
| A | THR85 |
Functional Information from PROSITE/UniProt
| site_id | PS00159 |
| Number of Residues | 10 |
| Details | ALDOLASE_KDPG_KHG_1 KDPG and KHG aldolases active site. GIrtlEVTLR |
| Chain | Residue | Details |
| A | GLY52-ARG61 |
| site_id | PS00160 |
| Number of Residues | 14 |
| Details | ALDOLASE_KDPG_KHG_2 KDPG and KHG aldolases Schiff-base forming residue. GyrrFKLFPAeisG |
| Chain | Residue | Details |
| A | GLY140-GLY153 |
| site_id | PS00165 |
| Number of Residues | 14 |
| Details | DEHYDRATASE_SER_THR Serine/threonine dehydratases pyridoxal-phosphate attachment site. Eisgg.VAAIKAFGG |
| Chain | Residue | Details |
| A | GLU150-GLY163 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P0A955","evidenceCode":"ECO:0000250"}]} |
| 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":"12876349","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"6988426","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"7161801","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P0A955","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"covalent","evidences":[{"source":"UniProtKB","id":"P0A955","evidenceCode":"ECO:0000250"}]} |
| 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":"UniProtKB","id":"P0A955","evidenceCode":"ECO:0000250"}]} |
| 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 | LYS145 | |
| A | GLU57 |
