4X4M
Structure of FcgammaRI in complex with Fc reveals the importance of glycan recognition for high affinity IgG binding
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A, B, C, D (A, B, C, D) | Ig gamma-1 chain C region | polymer | 219 | 24699.0 | 4 | UniProt (P01857) Pfam (PF07654) | Homo sapiens (Human) | |
| 2 | E, F (E, F) | High affinity immunoglobulin gamma Fc receptor I | polymer | 275 | 31014.1 | 2 | UniProt (P12314) Pfam (PF13927) Pfam (PF13895) Pfam (PF00047) | Homo sapiens (Human) | IgG Fc receptor I,Fc-gamma RI,FcRI,Fc-gamma RIA,FcgammaRIa |
| 3 | G, H (G, H) | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[beta-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose | branched | 1463.3 | 2 | In PDB GlyTouCan (G59451NL) | |||
| 4 | I (I) | beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[beta-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose | branched | 1625.5 | 1 | In PDB GlyTouCan (G33244HE) | |||
| 5 | J (J) | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | branched | 1114.0 | 1 | In PDB GlyTouCan (G55061AW) | |||
| 6 | K (K) | N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose | branched | 471.4 | 1 | In PDB GlyTouCan (G30207PZ) | |||
| 7 | L (D) | 2-acetamido-2-deoxy-beta-D-glucopyranose | non-polymer | 221.2 | 1 | Chemie (NAG) | |||
| 8 | M (D) | beta-L-fucopyranose | non-polymer | 164.2 | 1 | Chemie (FUL) |
Sequence modifications
E, F: 21 - 289 (UniProt: P12314)
| PDB | External Database | Details |
|---|---|---|
| Lys 25 | Thr 25 | engineered mutation |
| Ser 38 | Thr 38 | engineered mutation |
| Pro 46 | Leu 46 | engineered mutation |
| Ile 63 | Thr 63 | engineered mutation |
| Thr 69 | Ser 69 | engineered mutation |
| His 71 | Arg 71 | engineered mutation |
| Glu 77 | Val 77 | engineered mutation |
| Asp 78 | Asn 78 | engineered mutation |
| Val 100 | Ile 100 | engineered mutation |
| Leu 114 | Phe 114 | engineered mutation |
| Met 160 | Ile 160 | engineered mutation |
| Ser 163 | Asn 163 | engineered mutation |
| Thr 195 | Asn 195 | engineered mutation |
| Thr 206 | Asn 206 | engineered mutation |
| Pro 207 | Leu 207 | engineered mutation |
| Asp 240 | Asn 240 | engineered mutation |
| His 283 | Leu 283 | engineered mutation |
| Gln 285 | Leu 285 | engineered mutation |
| His 290 | - | expression tag |
| His 291 | - | expression tag |
| His 292 | - | expression tag |
| His 293 | - | expression tag |
| His 294 | - | expression tag |
| His 295 | - | expression tag |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 6 |
| Total formula weight | 160824.0 | |
| Branched | Number of molecules | 5 |
| Total formula weight | 6137.6 | |
| Non-Polymers* | Number of molecules | 2 |
| Total formula weight | 385.4 | |
| All* | Total formula weight | 167346.9 |
