7CCZ
Crystal structure of the ES2 intermediate form of human hydroxymethylbilane synthase
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 | 
| 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 | 
Functional Information from PDB Data
| site_id | AC1 | 
| Number of Residues | 32 | 
| Details | binding site for residue 7J8 A 401 | 
| Chain | Residue | 
| A | SER96 | 
| A | ARG150 | 
| A | ARG173 | 
| A | LEU188 | 
| A | ALA189 | 
| A | ARG195 | 
| A | ALA214 | 
| A | VAL215 | 
| A | GLN217 | 
| A | GLY218 | 
| A | LEU254 | 
| A | LYS98 | 
| A | CYS261 | 
| A | SER262 | 
| A | HOH503 | 
| A | HOH504 | 
| A | HOH524 | 
| A | HOH530 | 
| A | HOH548 | 
| A | HOH559 | 
| A | HOH577 | 
| A | HOH578 | 
| A | ASP99 | 
| A | HOH593 | 
| A | HOH607 | 
| A | HOH644 | 
| A | LEU100 | 
| A | PRO101 | 
| A | THR102 | 
| A | SER146 | 
| A | SER147 | 
| A | ARG149 | 
| site_id | AC2 | 
| Number of Residues | 32 | 
| Details | binding site for Di-peptide 7J8 B 401 and CYS B 261 | 
| Chain | Residue | 
| B | SER96 | 
| B | LYS98 | 
| B | ASP99 | 
| B | LEU100 | 
| B | PRO101 | 
| B | THR102 | 
| B | SER146 | 
| B | SER147 | 
| B | ARG149 | 
| B | ARG150 | 
| B | ARG173 | 
| B | LEU188 | 
| B | ALA189 | 
| B | ARG195 | 
| B | VAL215 | 
| B | GLN217 | 
| B | GLY218 | 
| B | LEU254 | 
| B | GLY260 | 
| B | SER262 | 
| B | VAL263 | 
| B | HOH505 | 
| B | HOH510 | 
| B | HOH516 | 
| B | HOH518 | 
| B | HOH538 | 
| B | HOH547 | 
| B | HOH554 | 
| B | HOH582 | 
| B | HOH592 | 
| B | HOH598 | 
| B | HOH628 | 
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 | 1 | 
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P22907","evidenceCode":"ECO:0000250"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI2 | 
| Number of Residues | 2 | 
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI3 | 
| Number of Residues | 2 | 
| Details | Modified residue: {"description":"S-(dipyrrolylmethanemethyl)cysteine","evidences":[{"source":"PubMed","id":"18936296","evidenceCode":"ECO:0000269"}]} | 
| Chain | Residue | Details | 











