5JIK
Crystal structure of HER2 binding IgG1-Fc (Fcab H10-03-6)
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A, B (A, B) | Ig gamma-1 chain C region | polymer | 227 | 25641.1 | 2 | UniProt (P01857) Pfam (PF07654) | Homo sapiens (Human) | |
| 2 | C (C) | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | branched | 1114.0 | 1 | In PDB GlyTouCan (G64481DJ) | |||
| 3 | D (D) | alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | branched | 910.8 | 1 | In PDB GlyTouCan (G22768VO) | |||
| 4 | E, F (A, B) | water | water | 18.0 | 106 | Chemie (HOH) |
Sequence modifications
A, B: 225 - 446 (UniProt: P01857)
| PDB | External Database | Details |
|---|---|---|
| Tyr 358 | Leu 241 | engineered mutation |
| Leu 359 | Thr 242 | engineered mutation |
| Tyr 360 | Lys 243 | engineered mutation |
| Gly 361 | Asn 244 | engineered mutation |
| Asp 362 | Gln 245 | engineered mutation |
| Pro 413 | Asp 296 | engineered mutation |
| Arg 414 | Lys 297 | engineered mutation |
| His 415 | Ser 298 | engineered mutation |
| Ser 415 | - | insertion |
| Ala 415 | - | insertion |
| Arg 415 | - | insertion |
| Met 415 | - | insertion |
| Trp 415 | - | insertion |
| Ala 418 | Gln 301 | engineered mutation |
| His 419 | Gln 302 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 2 |
| Total formula weight | 51282.1 | |
| Branched | Number of molecules | 2 |
| Total formula weight | 2024.8 | |
| All* | Total formula weight | 53307.0 |
