4HI4
Crystal structure of the 5-coordinate ferric heme-binding PAS domain of Aer2 from P. aeruginosa
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE HEM A 301 |
| Chain | Residue |
| A | MET187 |
| A | LEU255 |
| A | LEU257 |
| A | VAL281 |
| A | ILE195 |
| A | PHE233 |
| A | HIS234 |
| A | LYS235 |
| A | HIS239 |
| A | GLN240 |
| A | HIS251 |
| A | ALA253 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 302 |
| Chain | Residue |
| A | ASP231 |
| A | HIS234 |
| G | GLU254 |
| G | SER263 |
| G | ARG286 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE HEM B 301 |
| Chain | Residue |
| B | MET187 |
| B | ILE195 |
| B | PHE233 |
| B | HIS234 |
| B | LYS235 |
| B | HIS239 |
| B | GLN240 |
| B | HIS251 |
| B | ALA253 |
| B | LEU255 |
| B | LEU257 |
| B | VAL281 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GOL B 302 |
| Chain | Residue |
| B | LEU179 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE HEM D 301 |
| Chain | Residue |
| B | PRO218 |
| D | ILE195 |
| D | ILE230 |
| D | PHE233 |
| D | HIS234 |
| D | LYS235 |
| D | GLN240 |
| D | LEU244 |
| D | HIS251 |
| D | ALA253 |
| D | LEU255 |
| D | LEU257 |
| D | VAL281 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL D 302 |
| Chain | Residue |
| D | HIS171 |
| D | ILE175 |
| D | VAL269 |
| D | PHE270 |
| D | HOH413 |
| site_id | AC7 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE HEM G 301 |
| Chain | Residue |
| G | ILE195 |
| G | ILE230 |
| G | PHE233 |
| G | HIS234 |
| G | LYS235 |
| G | GLN240 |
| G | LEU244 |
| G | HIS251 |
| G | ALA253 |
| G | LEU255 |
| G | LEU257 |
| G | VAL281 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL G 302 |
| Chain | Residue |
| A | GLN282 |
| G | ALA184 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL G 303 |
| Chain | Residue |
| G | ILE175 |
| G | LEU179 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 168 |
| Details | Domain: {"description":"PAS","evidences":[{"source":"PROSITE-ProRule","id":"PRU00140","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Motif: {"description":"DxT. Important for signal propagation","evidences":[{"source":"PubMed","id":"34383467","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"22622145","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23274111","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3VOL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4HI4","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Site: {"description":"Important for gas binding and signaling","evidences":[{"source":"PubMed","id":"28167524","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Site: {"description":"Plays a crucial role in stabilization of the heme-bound O(2)","evidences":[{"source":"PubMed","id":"22622145","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28167524","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
