2GSA
CRYSTAL STRUCTURE OF GLUTAMATE-1-SEMIALDEHYDE AMINOMUTASE (AMINOTRANSFERASE, WILD-TYPE FORM)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006779 | biological_process | porphyrin-containing compound biosynthetic process |
| A | 0006782 | biological_process | protoporphyrinogen IX biosynthetic process |
| A | 0008483 | molecular_function | transaminase activity |
| 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 |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006779 | biological_process | porphyrin-containing compound biosynthetic process |
| B | 0006782 | biological_process | protoporphyrinogen IX biosynthetic process |
| B | 0008483 | molecular_function | transaminase activity |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PMP A 500 |
| Chain | Residue |
| A | MET248 |
| A | LYS273 |
| A | HOH2110 |
| A | HOH2207 |
| A | HOH2208 |
| B | THR305 |
| B | HOH2015 |
| A | GLY123 |
| A | THR124 |
| A | TYR150 |
| A | GLY152 |
| A | ASN217 |
| A | ASP245 |
| A | VAL247 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PLP B 434 |
| Chain | Residue |
| A | THR305 |
| B | SER122 |
| B | GLY123 |
| B | THR124 |
| B | TYR150 |
| B | GLY152 |
| B | GLU212 |
| B | ASN217 |
| B | ASP245 |
| B | VAL247 |
| B | MET248 |
| B | LYS273 |
| B | HOH2024 |
| B | HOH2101 |
| B | HOH2163 |
| B | HOH2168 |
| site_id | COA |
| Number of Residues | 1 |
| Details | AS HETATM 500 IN ACTIVE SITE OF CHAIN A. |
| Chain | Residue |
| A | PMP500 |
| site_id | COB |
| Number of Residues | 1 |
| Details | SCHIFF BASE LINKAGE TO LYS 273 IN CHAIN B. |
| Chain | Residue |
| B | PLP434 |
Functional Information from PROSITE/UniProt
| site_id | PS00600 |
| Number of Residues | 37 |
| Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LVfDEVmt.GF.RiAyggvqekfgvtp....DLTtlGKiigGG |
| Chain | Residue | Details |
| A | LEU242-GLY278 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 9144156 |
| Chain | Residue | Details |
| A | LYS273 | |
| A | ASP245 | |
| A | TYR150 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 9144156 |
| Chain | Residue | Details |
| B | LYS273 | |
| B | ASP245 | |
| B | TYR150 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 195 |
| Chain | Residue | Details |
| A | TYR150 | steric role |
| A | ASP245 | electrostatic stabiliser, hydrogen bond acceptor |
| A | LYS273 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 195 |
| Chain | Residue | Details |
| B | TYR150 | steric role |
| B | ASP245 | electrostatic stabiliser, hydrogen bond acceptor |
| B | LYS273 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
