1PDA
STRUCTURE OF PORPHOBILINOGEN DEAMINASE REVEALS A FLEXIBLE MULTIDOMAIN POLYMERASE WITH A SINGLE CATALYTIC SITE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004418 | molecular_function | hydroxymethylbilane synthase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006779 | biological_process | porphyrin-containing compound biosynthetic process |
| A | 0006782 | biological_process | protoporphyrinogen IX biosynthetic process |
| A | 0006783 | biological_process | heme biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0018160 | biological_process | peptidyl-pyrromethane cofactor linkage |
| A | 0033014 | biological_process | tetrapyrrole biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE DPM A 314 |
| Chain | Residue |
| A | ARG131 |
| A | ARG132 |
| A | ARG149 |
| A | GLY150 |
| A | ASN151 |
| A | VAL152 |
| A | ARG155 |
| A | CYS242 |
| A | HOH402 |
| A | ARG11 |
| A | SER13 |
| A | PHE62 |
| A | LYS83 |
| A | ASP84 |
| A | THR127 |
| A | SER128 |
| A | SER129 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACY A 315 |
| Chain | Residue |
| A | LYS83 |
| A | ARG132 |
| A | LEU169 |
| A | ALA170 |
| A | HOH468 |
| site_id | DPM |
| Number of Residues | 1 |
| Details |
| Chain | Residue |
| A | CYS242 |
Functional Information from PROSITE/UniProt
| site_id | PS00533 |
| Number of Residues | 17 |
| Details | PORPHOBILINOGEN_DEAM Porphobilinogen deaminase cofactor-binding site. ERaMntrLeGACqVPIG |
| Chain | Residue | Details |
| A | GLU231-GLY247 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | MOD_RES: S-(dipyrrolylmethanemethyl)cysteine |
| Chain | Residue | Details |
| A | CYS242 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 260 |
| Chain | Residue | Details |
| A | LYS83 | activator, electrostatic stabiliser, hydrogen bond donor |
| A | ASP84 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | ARG131 | activator, electrostatic stabiliser, hydrogen bond donor |
| A | ARG132 | activator, electrostatic stabiliser, hydrogen bond donor |
| A | ARG149 | activator, electrostatic stabiliser |
| A | ARG155 | activator, electrostatic stabiliser |
| A | CYS242 | covalently attached |
