9FBU
X-ray structure of the iGluSnFR3 in complex with L-glutamate
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A (A) | Periplasmic binding transport protein,Green fluorescent protein | polymer | 520 | 58029.4 | 1 | UniProt (A0A0H2UXX1) UniProt (P42212) Pfam (PF00497) | Shigella flexneri | |
| 2 | B (A) | GLUTAMIC ACID | non-polymer | 147.1 | 1 | Chemie (GLU) | |||
| 3 | C (A) | water | water | 18.0 | 334 | Chemie (HOH) |
Sequence modifications
A: 2 - 250 (UniProt: A0A0H2UXX1)
A: 251 - 342 (UniProt: P42212)
A: 349 - 496 (UniProt: P42212)
A: 497 - 520 (UniProt: A0A0H2UXX1)
| PDB | External Database | Details |
|---|---|---|
| Gly 1 | - | expression tag |
| Asp 22 | Glu 48 | engineered mutation |
| Ser 32 | Asn 58 | engineered mutation |
| His 34 | Gln 60 | engineered mutation |
| Glu 42 | Asp 68 | engineered mutation |
| Tyr 81 | Phe 107 | engineered mutation |
| Asn 124 | Asp 150 | engineered mutation |
| Asp 127 | Gly 153 | engineered mutation |
| Ser 181 | Ala 207 | engineered mutation |
| Asp 195 | Asn 221 | engineered mutation |
| Glu 197 | Asp 223 | engineered mutation |
| Leu 249 | Pro 275 | engineered mutation |
| Val 250 | Pro 276 | engineered mutation |
| PDB | External Database | Details |
|---|---|---|
| Asn 251 | Ser 147 | engineered mutation |
| Thr 253 | Asn 149 | engineered mutation |
| Thr 257 | Met 153 | engineered mutation |
| Ala 267 | Val 163 | engineered mutation |
| His 272 | Arg 168 | engineered mutation |
| Val 275 | Ile 171 | engineered mutation |
| Tyr 307 | Thr 203 | engineered mutation |
| Val 310 | Ala 206 | engineered mutation |
| Thr 331 | Ala 227 | engineered mutation |
| Asn 333 | Ile 229 | engineered mutation |
| Ser 334 | Thr 230 | engineered mutation |
| Leu 335 | His 231 | engineered mutation |
| PDB | External Database | Details |
|---|---|---|
| Gly 343 | - | linker |
| Gly 344 | - | linker |
| Thr 345 | - | linker |
| Gly 346 | - | linker |
| Gly 347 | - | linker |
| Ser 348 | - | linker |
| Arg 378 | Ser 30 | engineered mutation |
| Asn 387 | Tyr 39 | engineered mutation |
| Leu 412 | Phe 64 | engineered mutation |
| Gys 413 | Ser 65 | chromophore |
| Gys 413 | Tyr 66 | chromophore |
| Gys 413 | Gly 67 | chromophore |
| Ala 420 | Ser 72 | engineered mutation |
| Ser 447 | Phe 99 | engineered mutation |
| Thr 453 | Asn 105 | engineered mutation |
| Leu 462 | Phe 114 | engineered mutation |
| Phe 493 | Tyr 145 | engineered mutation |
| Asn 495 | Ser 147 | engineered mutation |
| Pro 496 | His 148 | engineered mutation |
| PDB | External Database | Details |
|---|---|---|
| Lys 520 | Asn 302 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 1 |
| Total formula weight | 58029.4 | |
| Non-Polymers* | Number of molecules | 1 |
| Total formula weight | 147.1 | |
| All* | Total formula weight | 58176.5 |






