5I92
Crystal structure of Glutamate-1-semialdehyde 2,1- aminomutase (GSA) from Pseudomonas aeruginosa
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 | 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 | 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 |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006779 | biological_process | porphyrin-containing compound biosynthetic process |
| C | 0006782 | biological_process | protoporphyrinogen IX biosynthetic process |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0033014 | biological_process | tetrapyrrole biosynthetic process |
| C | 0042286 | molecular_function | glutamate-1-semialdehyde 2,1-aminomutase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006779 | biological_process | porphyrin-containing compound biosynthetic process |
| D | 0006782 | biological_process | protoporphyrinogen IX biosynthetic process |
| D | 0008483 | molecular_function | transaminase activity |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0033014 | biological_process | tetrapyrrole biosynthetic process |
| D | 0042286 | molecular_function | glutamate-1-semialdehyde 2,1-aminomutase activity |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0006779 | biological_process | porphyrin-containing compound biosynthetic process |
| E | 0006782 | biological_process | protoporphyrinogen IX biosynthetic process |
| E | 0008483 | molecular_function | transaminase activity |
| E | 0016853 | molecular_function | isomerase activity |
| E | 0030170 | molecular_function | pyridoxal phosphate binding |
| E | 0033014 | biological_process | tetrapyrrole biosynthetic process |
| E | 0042286 | molecular_function | glutamate-1-semialdehyde 2,1-aminomutase activity |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0006779 | biological_process | porphyrin-containing compound biosynthetic process |
| F | 0006782 | biological_process | protoporphyrinogen IX biosynthetic process |
| F | 0008483 | molecular_function | transaminase activity |
| F | 0016853 | molecular_function | isomerase activity |
| F | 0030170 | molecular_function | pyridoxal phosphate binding |
| F | 0033014 | biological_process | tetrapyrrole biosynthetic process |
| F | 0042286 | molecular_function | glutamate-1-semialdehyde 2,1-aminomutase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 501 |
| Chain | Residue |
| A | SER114 |
| A | GLY115 |
| A | THR116 |
| A | TYR142 |
| B | SER113 |
| B | GLU117 |
| B | GLY296 |
| B | THR297 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 502 |
| Chain | Residue |
| A | GLY356 |
| A | LEU357 |
| A | ALA394 |
| A | GLU399 |
| A | GLY401 |
| A | HOH627 |
| A | ASN211 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue EDO B 501 |
| Chain | Residue |
| B | ASN211 |
| B | PHE355 |
| B | LEU357 |
| B | LEU393 |
| B | ALA394 |
| B | GLU399 |
| B | GLY401 |
| B | HOH666 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue GOL C 501 |
| Chain | Residue |
| C | SER114 |
| C | GLY115 |
| C | THR116 |
| C | TYR142 |
| D | SER113 |
| D | GLU117 |
| D | GLY296 |
| D | THR297 |
| D | HOH604 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue EDO C 502 |
| Chain | Residue |
| C | ASN211 |
| C | PHE355 |
| C | LEU357 |
| C | LEU393 |
| C | ALA394 |
| C | GLY401 |
| C | HOH661 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue EDO C 503 |
| Chain | Residue |
| C | SER84 |
| C | LEU298 |
| C | ASN301 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue EDO D 501 |
| Chain | Residue |
| D | ASN211 |
| D | PHE355 |
| D | LEU357 |
| D | LEU393 |
| D | ALA394 |
| D | GLY401 |
| D | HOH659 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue EDO D 502 |
| Chain | Residue |
| C | HOH631 |
| D | SER114 |
| D | GLY115 |
| D | THR116 |
| D | TYR142 |
| D | HOH736 |
| D | HOH862 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue EDO E 501 |
| Chain | Residue |
| E | ASN211 |
| E | PHE355 |
| E | LEU357 |
| E | LEU393 |
| E | ALA394 |
| E | GLY401 |
| E | HOH654 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue LEU F 501 |
| Chain | Residue |
| F | ARG381 |
| F | ALA422 |
| F | PHE423 |
| F | ALA424 |
| F | ALA425 |
| F | HOH643 |
| F | HOH894 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue EDO F 502 |
| Chain | Residue |
| F | ASN211 |
| F | PHE355 |
| F | LEU357 |
| F | LEU393 |
| F | ALA394 |
| F | GLY401 |
| F | HOH647 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue EDO F 503 |
| Chain | Residue |
| F | GLU139 |
| F | THR178 |
| F | LEU179 |
| F | PRO180 |
| F | HOH635 |
| F | HOH695 |
| site_id | AD4 |
| Number of Residues | 2 |
| Details | binding site for residue EDO F 504 |
| Chain | Residue |
| F | LYS27 |
| F | HOH843 |
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.RvAlggaqayygvtp....DLStfGKiigGG |
| Chain | Residue | Details |
| A | LEU234-GLY270 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250 |
| Chain | Residue | Details |
| A | LYS265 | |
| B | LYS265 | |
| C | LYS265 | |
| D | LYS265 | |
| E | LYS265 | |
| F | LYS265 |
