5HDM
Crystal structure of Arabidopsis thaliana glutamate-1-semialdehyde-2,1-aminomutase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005829 | cellular_component | cytosol |
| A | 0006782 | biological_process | protoporphyrinogen IX biosynthetic process |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009507 | cellular_component | chloroplast |
| A | 0009536 | cellular_component | plastid |
| A | 0009570 | cellular_component | chloroplast stroma |
| A | 0009941 | cellular_component | chloroplast envelope |
| A | 0015995 | biological_process | chlorophyll biosynthetic process |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0033014 | biological_process | tetrapyrrole biosynthetic process |
| A | 0042286 | molecular_function | glutamate-1-semialdehyde 2,1-aminomutase activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0048046 | cellular_component | apoplast |
| B | 0005829 | cellular_component | cytosol |
| B | 0006782 | biological_process | protoporphyrinogen IX biosynthetic process |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0009507 | cellular_component | chloroplast |
| B | 0009536 | cellular_component | plastid |
| B | 0009570 | cellular_component | chloroplast stroma |
| B | 0009941 | cellular_component | chloroplast envelope |
| B | 0015995 | biological_process | chlorophyll biosynthetic process |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0033014 | biological_process | tetrapyrrole biosynthetic process |
| B | 0042286 | molecular_function | glutamate-1-semialdehyde 2,1-aminomutase activity |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0048046 | cellular_component | apoplast |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | binding site for residue PMP A 500 |
| Chain | Residue |
| A | SER123 |
| A | MET249 |
| A | LYS274 |
| A | HOH741 |
| A | HOH815 |
| B | THR306 |
| B | HOH742 |
| A | GLY124 |
| A | THR125 |
| A | TYR151 |
| A | GLY153 |
| A | GLU213 |
| A | ASN218 |
| A | ASP246 |
| A | VAL248 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | binding site for residue PMP B 502 |
| Chain | Residue |
| A | THR306 |
| B | SER123 |
| B | GLY124 |
| B | THR125 |
| B | TYR151 |
| B | GLY153 |
| B | GLU213 |
| B | ASN218 |
| B | ASP246 |
| B | MET249 |
| B | LYS274 |
| B | PLP501 |
| B | HOH636 |
| B | HOH676 |
| B | HOH710 |
| B | HOH799 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | binding site for Di-peptide PLP B 501 and LYS B 274 |
| Chain | Residue |
| A | THR306 |
| B | TRP68 |
| B | PRO70 |
| B | SER123 |
| B | GLY124 |
| B | THR125 |
| B | TYR151 |
| B | GLU213 |
| B | ASN218 |
| B | ASP246 |
| B | VAL248 |
| B | MET249 |
| B | GLY273 |
| B | ILE275 |
| B | ILE276 |
| B | GLY277 |
| B | GLY278 |
| B | VAL282 |
| B | PMP502 |
| B | HOH676 |
| B | HOH691 |
| B | HOH710 |
| B | HOH799 |
| B | HOH883 |
Functional Information from PROSITE/UniProt
| site_id | PS00600 |
| Number of Residues | 37 |
| Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIfDEVmt.GF.RlAyggaqeyfgitp....DLTtlGKiigGG |
| Chain | Residue | Details |
| A | LEU243-GLY279 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:27303897, ECO:0007744|PDB:5HDM |
| Chain | Residue | Details |
| A | LYS274 | |
| B | LYS274 |
