3S5N
Crystal Structure of Human 4-hydroxy-2-oxoglutarate Aldolase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0008700 | molecular_function | 4-hydroxy-2-oxoglutarate aldolase activity |
| A | 0008747 | molecular_function | N-acetylneuraminate lyase activity |
| A | 0009436 | biological_process | glyoxylate catabolic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016833 | molecular_function | oxo-acid-lyase activity |
| A | 0019262 | biological_process | N-acetylneuraminate catabolic process |
| A | 0019470 | biological_process | 4-hydroxyproline catabolic process |
| A | 0033609 | biological_process | oxalate metabolic process |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0042866 | biological_process | pyruvate biosynthetic process |
| A | 0044281 | biological_process | small molecule metabolic process |
| A | 0046487 | biological_process | glyoxylate metabolic process |
| A | 0106009 | molecular_function | (4S)-4-hydroxy-2-oxoglutarate aldolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K A 330 |
| Chain | Residue |
| A | SER187 |
| A | HIS189 |
| A | ILE192 |
| A | ASP216 |
| A | HOH353 |
| A | HOH370 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 331 |
| Chain | Residue |
| A | HOH383 |
| A | HOH384 |
| A | THR212 |
| A | GLN215 |
| A | PHE217 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 1 |
| Chain | Residue |
| A | EDO2 |
| A | LYS63 |
| A | PHE295 |
| A | GLY296 |
| A | TYR297 |
| A | HOH381 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 2 |
| Chain | Residue |
| A | EDO1 |
| A | LYS63 |
| A | HOH380 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 3 |
| Chain | Residue |
| A | VAL42 |
| A | THR43 |
| A | PRO45 |
| A | ASN60 |
| A | ASN244 |
| A | MET292 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 4 |
| Chain | Residue |
| A | EDO6 |
| A | GLY143 |
| A | ARG144 |
| A | THR280 |
| A | ARG281 |
| A | ARG282 |
| A | GLY284 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 5 |
| Chain | Residue |
| A | EDO6 |
| A | SER77 |
| A | TYR141 |
| A | ASN173 |
| A | THR280 |
| A | HOH385 |
| A | HOH386 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO A 6 |
| Chain | Residue |
| A | EDO4 |
| A | EDO5 |
| A | TYR141 |
| A | GLY143 |
| A | ARG144 |
| A | GLY284 |
| A | ILE285 |
| A | PRO286 |
| A | LEU306 |
Functional Information from PROSITE/UniProt
| site_id | PS00666 |
| Number of Residues | 31 |
| Details | DHDPS_2 Dihydrodipicolinate synthase signature 2. YSVPanTgldLpvdavvtlsqhpn.IvGMKDS |
| Chain | Residue | Details |
| A | TYR168-SER198 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Schiff-base intermediate with substrate => ECO:0000269|PubMed:21998747 |
| Chain | Residue | Details |
| A | LYS196 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | SER198 | |
| A | GLY222 | |
| A | SER77 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | SITE: Involved in proton transfer during cleavage |
| Chain | Residue | Details |
| A | TYR168 |
