4MU1
The structure of wt A. thaliana IGPD2 in complex with Mn2+, imidazole, and sulfate at 1.5 A resolution
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 301 |
| Chain | Residue |
| A | HIS47 |
| A | HIS74 |
| A | HIS169 |
| A | GLU173 |
| A | IMD303 |
| A | HOH404 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 302 |
| Chain | Residue |
| A | HIS170 |
| A | IMD303 |
| A | HOH401 |
| A | HIS73 |
| A | GLU77 |
| A | HIS145 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE IMD A 303 |
| Chain | Residue |
| A | HIS73 |
| A | GLU77 |
| A | LEU107 |
| A | HIS170 |
| A | GLU173 |
| A | MN301 |
| A | MN302 |
| A | HOH401 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 304 |
| Chain | Residue |
| A | ARG161 |
| A | ARG161 |
| A | ARG161 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 305 |
| Chain | Residue |
| A | GLN51 |
| A | HIS55 |
| A | ARG99 |
| A | LYS177 |
| A | HOH495 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 306 |
| Chain | Residue |
| A | GLU18 |
| A | ASN23 |
| A | ASN23 |
| A | SER25 |
| A | ARG63 |
| A | HOH528 |
| A | HOH542 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 307 |
| Chain | Residue |
| A | LEU88 |
| A | ARG94 |
| A | LEU118 |
| A | SER119 |
| A | GLY120 |
| A | SER154 |
| A | GLY155 |
| A | HOH503 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 308 |
| Chain | Residue |
| A | GLU93 |
| A | ARG94 |
| A | LYS95 |
| A | HOH444 |
| A | HOH565 |
Functional Information from PROSITE/UniProt
| site_id | PS00954 |
| Number of Residues | 14 |
| Details | IGP_DEHYDRATASE_1 Imidazoleglycerol-phosphate dehydratase signature 1. IDdHHtnEdvALAI |
| Chain | Residue | Details |
| A | ILE70-ILE83 |
| site_id | PS00955 |
| Number of Residues | 13 |
| Details | IGP_DEHYDRATASE_2 Imidazoleglycerol-phosphate dehydratase signature 2. GkNsHHiiEAtFK |
| Chain | Residue | Details |
| A | GLY165-LYS177 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:27717128, ECO:0007744|PDB:5EKW, ECO:0007744|PDB:5EL9, ECO:0007744|PDB:5ELW |
| Chain | Residue | Details |
| A | GLU21 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:26095028, ECO:0000269|PubMed:27717128, ECO:0007744|PDB:4MU0, ECO:0007744|PDB:4MU1, ECO:0007744|PDB:4MU4, ECO:0007744|PDB:4QNJ, ECO:0007744|PDB:4QNK, ECO:0007744|PDB:5EKW, ECO:0007744|PDB:5EL9, ECO:0007744|PDB:5ELW |
| Chain | Residue | Details |
| A | HIS47 | |
| A | HIS74 | |
| A | HIS169 | |
| A | GLU173 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:26095028, ECO:0000269|PubMed:27717128, ECO:0007744|PDB:4MU0, ECO:0007744|PDB:4MU3, ECO:0007744|PDB:4MU4, ECO:0007744|PDB:4QNJ, ECO:0007744|PDB:4QNK, ECO:0007744|PDB:5ELW |
| Chain | Residue | Details |
| A | HIS73 | |
| A | GLU77 | |
| A | HIS145 | |
| A | HIS170 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:26095028, ECO:0000269|PubMed:27717128, ECO:0007744|PDB:4MU3, ECO:0007744|PDB:4MU4, ECO:0007744|PDB:4QNK, ECO:0007744|PDB:5EKW, ECO:0007744|PDB:5EL9, ECO:0007744|PDB:5ELW |
| Chain | Residue | Details |
| A | ARG99 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:26095028, ECO:0000269|PubMed:27717128, ECO:0007744|PDB:4MU4, ECO:0007744|PDB:5EKW, ECO:0007744|PDB:5EL9, ECO:0007744|PDB:5ELW |
| Chain | Residue | Details |
| A | ARG121 | |
| A | SER199 |
