3FQA
Gabaculien complex of gabaculine resistant GSAM version
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005737 | cellular_component | cytoplasm |
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 | 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 A1434 |
Chain | Residue |
A | GLY1123 |
A | HOH7052 |
A | HOH7192 |
A | HOH7245 |
B | GLY2304 |
B | THR2305 |
A | THR1124 |
A | TYR1150 |
A | ASN1217 |
A | ASP1245 |
A | VAL1247 |
A | ILE1248 |
A | LYS1273 |
A | GAB2000 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GAB A2000 |
Chain | Residue |
A | SER1029 |
A | ARG1032 |
A | TRP1067 |
A | TYR1150 |
A | PMP1434 |
A | HOH7245 |
B | ALA2303 |
B | GLY2304 |
B | THR2305 |
site_id | AC3 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE PMP B2434 |
Chain | Residue |
A | THR1305 |
B | SER2122 |
B | GLY2123 |
B | THR2124 |
B | TYR2150 |
B | GLU2212 |
B | ASN2217 |
B | ASP2245 |
B | VAL2247 |
B | ILE2248 |
B | LYS2273 |
B | HOH7095 |
B | HOH7096 |
B | HOH7097 |
B | HOH7139 |
Functional Information from PROSITE/UniProt
site_id | PS00600 |
Number of Residues | 37 |
Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LVfDEVit.GF.RiAyggvqekfgvtp....DLTtlGKiigGG |
Chain | Residue | Details |
A | LEU1242-GLY1278 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine |
Chain | Residue | Details |
A | LYS1273 | |
B | LYS2273 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1b8g |
Chain | Residue | Details |
A | ASP1245 | |
A | LYS1273 | |
A | TYR1150 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1b8g |
Chain | Residue | Details |
B | LYS2273 | |
B | TYR2150 | |
B | ASP2245 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1b8g |
Chain | Residue | Details |
A | ASP1245 | |
A | TYR1150 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1b8g |
Chain | Residue | Details |
B | TYR2150 | |
B | ASP2245 |
site_id | CSA5 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1b8g |
Chain | Residue | Details |
A | PHE1157 | |
A | ASP1245 | |
A | LYS1273 |
site_id | CSA6 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1b8g |
Chain | Residue | Details |
B | LYS2273 | |
B | PHE2157 | |
B | ASP2245 |
site_id | MCSA1 |
Number of Residues | 3 |
Details | M-CSA 195 |
Chain | Residue | Details |
A | TYR1150 | steric role |
A | ASP1245 | electrostatic stabiliser, hydrogen bond acceptor |
A | LYS1273 | 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 | TYR2150 | steric role |
B | ASP2245 | electrostatic stabiliser, hydrogen bond acceptor |
B | LYS2273 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |