5ELV
Crystal structure of the GluA2 ligand-binding domain (S1S2J-L504-N775) in complex with glutamate and BPAM-521 at 1.92 A resolution
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 301 |
| Chain | Residue |
| A | SER140 |
| A | LYS144 |
| A | ARG148 |
| A | HOH404 |
| A | HOH409 |
| A | HOH541 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 302 |
| Chain | Residue |
| A | HOH456 |
| A | HOH461 |
| B | LYS183 |
| A | ARG31 |
| A | HOH408 |
| A | HOH422 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 303 |
| Chain | Residue |
| A | ARG149 |
| A | HOH474 |
| B | LYS240 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 304 |
| Chain | Residue |
| A | ARG148 |
| A | TRP159 |
| A | ARG163 |
| A | HOH558 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 305 |
| Chain | Residue |
| A | SER108 |
| A | SER194 |
| A | THR195 |
| A | GLU198 |
| A | ASN214 |
| A | HOH465 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 306 |
| Chain | Residue |
| A | ARG163 |
| B | HOH577 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 307 |
| Chain | Residue |
| A | LYS21 |
| A | ASN22 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue ACT A 308 |
| Chain | Residue |
| A | ALA153 |
| B | LYS249 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue ACT A 309 |
| Chain | Residue |
| A | ASP257 |
| A | HOH431 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue ACT A 310 |
| Chain | Residue |
| A | ASP248 |
| B | ASN214 |
| B | ASP216 |
| B | SER217 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue ACT A 311 |
| Chain | Residue |
| A | ASP38 |
| A | GLU42 |
| A | LEU250 |
| A | LYS253 |
| B | LYS21 |
| site_id | AD3 |
| Number of Residues | 13 |
| Details | binding site for residue 5PX A 312 |
| Chain | Residue |
| A | PRO105 |
| A | SER108 |
| A | SER217 |
| A | LYS218 |
| A | GLY219 |
| A | HOH545 |
| B | LYS104 |
| B | PRO105 |
| B | PHE106 |
| B | MET107 |
| B | SER108 |
| B | SER242 |
| B | 5PX312 |
| site_id | AD4 |
| Number of Residues | 12 |
| Details | binding site for residue GLU A 313 |
| Chain | Residue |
| A | TYR61 |
| A | PRO89 |
| A | LEU90 |
| A | THR91 |
| A | ARG96 |
| A | GLY141 |
| A | SER142 |
| A | THR143 |
| A | GLU193 |
| A | HOH437 |
| A | HOH444 |
| A | HOH473 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 B 301 |
| Chain | Residue |
| B | SER140 |
| B | LYS144 |
| B | ARG148 |
| B | HOH411 |
| B | HOH430 |
| B | HOH458 |
| site_id | AD6 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 302 |
| Chain | Residue |
| B | SER108 |
| B | SER194 |
| B | GLU198 |
| B | ASN214 |
| B | HOH407 |
| site_id | AD7 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 303 |
| Chain | Residue |
| B | ARG148 |
| B | TRP159 |
| B | ARG163 |
| B | ACT307 |
| site_id | AD8 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 304 |
| Chain | Residue |
| B | LYS4 |
| B | THR5 |
| site_id | AD9 |
| Number of Residues | 2 |
| Details | binding site for residue ACT B 305 |
| Chain | Residue |
| B | LYS82 |
| B | LYS116 |
| site_id | AE1 |
| Number of Residues | 3 |
| Details | binding site for residue ACT B 306 |
| Chain | Residue |
| B | ASP58 |
| B | LYS60 |
| B | ASN72 |
| site_id | AE2 |
| Number of Residues | 3 |
| Details | binding site for residue ACT B 307 |
| Chain | Residue |
| B | LYS144 |
| B | ARG163 |
| B | GOL303 |
| site_id | AE3 |
| Number of Residues | 4 |
| Details | binding site for residue ACT B 308 |
| Chain | Residue |
| B | SER123 |
| B | ALA124 |
| B | GLY213 |
| B | HOH422 |
| site_id | AE4 |
| Number of Residues | 5 |
| Details | binding site for residue ACT B 309 |
| Chain | Residue |
| B | LYS240 |
| B | HOH504 |
| A | TYR94 |
| B | HIS46 |
| B | ALA237 |
| site_id | AE5 |
| Number of Residues | 5 |
| Details | binding site for residue PEG B 310 |
| Chain | Residue |
| B | GLU27 |
| B | GLY28 |
| B | ARG31 |
| B | LYS52 |
| B | HOH453 |
| site_id | AE6 |
| Number of Residues | 4 |
| Details | binding site for residue PEG B 311 |
| Chain | Residue |
| A | ARG203 |
| A | LYS258 |
| B | HIS23 |
| B | ARG31 |
| site_id | AE7 |
| Number of Residues | 12 |
| Details | binding site for residue 5PX B 312 |
| Chain | Residue |
| A | LYS104 |
| A | PRO105 |
| A | PHE106 |
| A | MET107 |
| A | SER108 |
| A | SER242 |
| A | 5PX312 |
| B | PRO105 |
| B | SER108 |
| B | SER217 |
| B | LYS218 |
| B | GLY219 |
| site_id | AE8 |
| Number of Residues | 12 |
| Details | binding site for residue GLU B 313 |
| Chain | Residue |
| B | TYR61 |
| B | PRO89 |
| B | LEU90 |
| B | THR91 |
| B | ARG96 |
| B | GLY141 |
| B | SER142 |
| B | THR143 |
| B | GLU193 |
| B | HOH462 |
| B | HOH465 |
| B | HOH467 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11086992","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16483599","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1FTJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CMO","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Site: {"description":"Interaction with the cone snail toxin Con-ikot-ikot","evidences":[{"source":"PubMed","id":"25103405","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Site: {"description":"Crucial to convey clamshell closure to channel opening","evidences":[{"source":"PubMed","id":"25103405","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by PKC","evidences":[{"source":"PubMed","id":"8848293","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by PKG","evidences":[{"source":"PubMed","id":"8848293","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |






