3VOL
X-ray Crystal Structure of PAS-HAMP Aer2 in the CN-bound Form
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE HEM A 401 |
Chain | Residue |
A | ALA189 |
A | ALA253 |
A | LEU255 |
A | TRP283 |
A | CYN402 |
A | HOH508 |
A | GLN216 |
A | ILE230 |
A | PHE233 |
A | HIS234 |
A | LYS235 |
A | HIS239 |
A | GLN240 |
A | HIS251 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CYN A 402 |
Chain | Residue |
A | LEU255 |
A | TRP283 |
A | HEM401 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | BINDING: axial binding residue => ECO:0000269|PubMed:22622145, ECO:0000269|PubMed:23274111, ECO:0007744|PDB:3VOL, ECO:0007744|PDB:4HI4 |
Chain | Residue | Details |
A | HIS234 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | SITE: Important for gas binding and signaling => ECO:0000269|PubMed:28167524 |
Chain | Residue | Details |
A | LEU264 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | SITE: Plays a crucial role in stabilization of the heme-bound O(2) => ECO:0000269|PubMed:22622145, ECO:0000269|PubMed:28167524 |
Chain | Residue | Details |
A | TRP283 |