2ZSM
Crystal structure of glutamate-1-semialdehyde 2,1-aminomutase from Aeropyrum pernix, hexagonal 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 | 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PMP A1001 |
| Chain | Residue |
| A | SER120 |
| A | GLY302 |
| A | THR303 |
| A | PHE304 |
| A | HOH1017 |
| A | HOH1037 |
| A | HOH1092 |
| A | GLY121 |
| A | THR122 |
| A | TYR148 |
| A | HIS149 |
| A | ASN215 |
| A | ASP243 |
| A | VAL246 |
| A | LYS271 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A1004 |
| Chain | Residue |
| A | HIS72 |
| A | LYS73 |
| A | GLY88 |
| A | TRP89 |
| A | LEU90 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PMP B1002 |
| Chain | Residue |
| B | SER120 |
| B | GLY121 |
| B | THR122 |
| B | TYR148 |
| B | HIS149 |
| B | GLU210 |
| B | ASN215 |
| B | ASP243 |
| B | VAL245 |
| B | VAL246 |
| B | LYS271 |
| B | HOH1017 |
| B | HOH1048 |
| B | HOH1067 |
| B | HOH1100 |
| C | GLY302 |
| C | THR303 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B1005 |
| Chain | Residue |
| B | HIS72 |
| B | LYS73 |
| C | TRP89 |
| C | LEU90 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PMP C1003 |
| Chain | Residue |
| B | GLY302 |
| B | THR303 |
| B | PHE304 |
| B | HOH1019 |
| B | HOH1025 |
| C | SER120 |
| C | GLY121 |
| C | THR122 |
| C | TYR148 |
| C | HIS149 |
| C | GLU210 |
| C | ASN215 |
| C | ASP243 |
| C | VAL246 |
| C | LYS271 |
| C | HOH1097 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL C1006 |
| Chain | Residue |
| B | TRP89 |
| B | LEU90 |
| C | HIS72 |
| C | LYS73 |
Functional Information from PROSITE/UniProt
| site_id | PS00600 |
| Number of Residues | 37 |
| Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIlDEVvt.GF.RlGlegaqgyfnieg....DIIvlGKiigGG |
| Chain | Residue | Details |
| A | LEU240-GLY276 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250 |
| Chain | Residue | Details |
| A | LYS271 | |
| B | LYS271 | |
| C | LYS271 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | ASP243 | |
| A | TYR148 | |
| A | LYS271 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | ASP243 | |
| B | TYR148 | |
| B | LYS271 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| C | ASP243 | |
| C | TYR148 | |
| C | LYS271 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | ASP243 |
| site_id | CSA5 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | ASP243 |
| site_id | CSA6 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| C | ASP243 |
