5ELW
A. thaliana IGPD2 in complex with the triazole-phosphonate inhibitor, (R)-C348, to 1.36A 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 | HIS73 |
| A | GLU77 |
| A | HIS145 |
| A | HIS170 |
| A | 5LD303 |
| A | HOH538 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue MN A 302 |
| Chain | Residue |
| A | GLU173 |
| A | 5LD303 |
| A | HIS47 |
| A | HIS74 |
| A | HIS169 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | binding site for residue 5LD A 303 |
| Chain | Residue |
| A | GLU21 |
| A | HIS47 |
| A | HIS73 |
| A | HIS74 |
| A | GLU77 |
| A | ARG99 |
| A | ARG121 |
| A | HIS169 |
| A | HIS170 |
| A | GLU173 |
| A | LYS177 |
| A | SER199 |
| A | LYS201 |
| A | MN301 |
| A | MN302 |
| A | HOH427 |
| A | HOH538 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 304 |
| Chain | Residue |
| A | ARG11 |
| A | LYS95 |
| A | SER189 |
| A | HOH403 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 305 |
| Chain | Residue |
| A | ASN23 |
| A | ASN23 |
| A | SER25 |
| A | HOH411 |
| A | HOH429 |
| A | HOH445 |
| A | HOH445 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | binding site for residue TRS A 306 |
| Chain | Residue |
| A | ASP102 |
| A | ASP102 |
| A | ASP102 |
| A | PHE103 |
| A | PHE103 |
| A | PHE103 |
| A | GLN185 |
| A | GLN185 |
| A | GLN185 |
| A | HOH518 |
| A | HOH518 |
| A | HOH518 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 307 |
| Chain | Residue |
| A | ARG161 |
| A | ARG161 |
| A | ARG161 |
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 |
