3EQ1
The Crystal Structure of Human Porphobilinogen Deaminase at 2.8A resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004418 | molecular_function | hydroxymethylbilane synthase activity |
| A | 0005515 | molecular_function | protein binding |
| 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 | 0006784 | biological_process | heme A biosynthetic process |
| A | 0006785 | biological_process | heme B biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0018160 | biological_process | peptidyl-pyrromethane cofactor linkage |
| A | 0033014 | biological_process | tetrapyrrole biosynthetic process |
| A | 0048034 | biological_process | heme O biosynthetic process |
| B | 0004418 | molecular_function | hydroxymethylbilane synthase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006779 | biological_process | porphyrin-containing compound biosynthetic process |
| B | 0006782 | biological_process | protoporphyrinogen IX biosynthetic process |
| B | 0006783 | biological_process | heme biosynthetic process |
| B | 0006784 | biological_process | heme A biosynthetic process |
| B | 0006785 | biological_process | heme B biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0018160 | biological_process | peptidyl-pyrromethane cofactor linkage |
| B | 0033014 | biological_process | tetrapyrrole biosynthetic process |
| B | 0048034 | biological_process | heme O biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE DPM A 400 |
| Chain | Residue |
| A | SER96 |
| A | ALA189 |
| A | ARG195 |
| A | ALA214 |
| A | GLY218 |
| A | CYS261 |
| A | LYS98 |
| A | ASP99 |
| A | SER146 |
| A | SER147 |
| A | ARG149 |
| A | ARG150 |
| A | ARG173 |
| A | LEU188 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE DPM B 401 |
| Chain | Residue |
| B | SER96 |
| B | LYS98 |
| B | ASP99 |
| B | SER146 |
| B | SER147 |
| B | ARG149 |
| B | ARG150 |
| B | ARG173 |
| B | LEU188 |
| B | ALA189 |
| B | ARG195 |
| B | GLY218 |
| B | CYS261 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 362 |
| Chain | Residue |
| A | ARG26 |
| A | SER28 |
| A | LEU30 |
| A | ALA31 |
| A | ASN169 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 363 |
| Chain | Residue |
| A | HIS120 |
| A | PRO208 |
| A | HIS268 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 364 |
| Chain | Residue |
| A | PRO119 |
| A | ARG246 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 362 |
| Chain | Residue |
| B | ARG26 |
| B | SER28 |
| B | ASN169 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 363 |
| Chain | Residue |
| B | HIS120 |
| B | HIS207 |
| B | PRO208 |
| B | HIS268 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 364 |
| Chain | Residue |
| B | PRO119 |
| B | ARG246 |
Functional Information from PROSITE/UniProt
| site_id | PS00533 |
| Number of Residues | 17 |
| Details | PORPHOBILINOGEN_DEAM Porphobilinogen deaminase cofactor-binding site. ERaFlrhLeGGCsVPVA |
| Chain | Residue | Details |
| A | GLU250-ALA266 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylserine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378 |
| Chain | Residue | Details |
| A | SER2 | |
| B | SER2 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER15 | |
| A | SER69 | |
| A | SER147 | |
| B | SER15 | |
| B | SER69 | |
| B | SER147 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P22907 |
| Chain | Residue | Details |
| A | LYS74 | |
| B | LYS74 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: S-(dipyrrolylmethanemethyl)cysteine => ECO:0000269|PubMed:18936296 |
| Chain | Residue | Details |
| A | CYS261 | |
| B | CYS261 |
