3TYG
Crystal structure of broad and potent HIV-1 neutralizing antibody PGT128 in complex with a glycosylated engineered gp120 outer domain with miniV3 (eODmV3)
Entity
Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
1 | A (A) | Envelope glycoprotein gp160 | polymer | 199 | 22019.5 | 1 | UniProt (P04578) UniProt (Q75760) Pfam (PF00516) | Human immunodeficiency virus 1 | |
2 | B (L) | PGT128 light chain, Ig lambda-2 chain C regions | polymer | 211 | 22206.6 | 1 | UniProt (P0CG05) Pfam (PF07654) UniProt (by SIFTS) (P0DOY2) | Homo sapiens (human) | |
3 | C (H) | PGT128 heavy chain, Ig gamma-1 chain C region | polymer | 239 | 25562.7 | 1 | UniProt (P01857) Pfam (PF07654) | Homo sapiens (human) | |
4 | D (B) | alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[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 | 1721.5 | 1 | In PDB GlyTouCan (G40702WU) | |||
5 | E (C) | alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]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 | 1235.1 | 1 | In PDB GlyTouCan (G55220VL) |
Sequence modifications
A: 1 - 8 (UniProt: P04578)
A: 15 - 47 (UniProt: P04578)
A: 57 - 100 (UniProt: P04578)
A: 101 - 108 (UniProt: Q75760)
A: 109 - 118 (UniProt: Q75760)
A: 119 - 190 (UniProt: P04578)
L: 1 - 106 (PDB: 3TYG)
L: 107 - 215 (UniProt: P0CG05)
H: 1 - 113 (PDB: 3TYG)
H: 114 - 231 (UniProt: P01857)
A: 15 - 47 (UniProt: P04578)
PDB | External Database | Details |
---|---|---|
Pro 9 | - | linker |
Ala 10 | - | linker |
Pro 11 | - | linker |
Pro 12 | - | linker |
Pro 13 | - | linker |
His 14 | - | linker |
Ile 23 | Leu 453 | engineered mutation |
PDB | External Database | Details |
---|---|---|
Ile 48 | - | linker |
Ala 49 | - | linker |
Arg 50 | - | linker |
Cys 51 | - | linker |
Gln 52 | - | linker |
Ile 53 | - | linker |
Ala 54 | - | linker |
Gly 55 | - | linker |
Thr 56 | - | linker |
Ser 86 | Thr 283 | engineered mutation |
Cys 88 | Ile 285 | engineered mutation |
PDB | External Database | Details |
---|---|---|
Pro 108 | Lys 302 | engineered mutation |
A: 119 - 190 (UniProt: P04578)
PDB | External Database | Details |
---|---|---|
Asp 175 | Asn 386 | engineered mutation |
Gly 191 | - | expression tag |
Thr 192 | - | expression tag |
Lys 193 | - | expression tag |
His 194 | - | expression tag |
His 195 | - | expression tag |
His 196 | - | expression tag |
His 197 | - | expression tag |
His 198 | - | expression tag |
His 199 | - | expression tag |
L: 107 - 215 (UniProt: P0CG05)
H: 1 - 113 (PDB: 3TYG)
H: 114 - 231 (UniProt: P01857)
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 3 |
Total formula weight | 69788.7 | |
Branched | Number of molecules | 2 |
Total formula weight | 2956.6 | |
All* | Total formula weight | 72745.4 |