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. 2010 Apr 27;27(8):1512–1529. doi: 10.1007/s11095-010-0143-5

Table I.

List of Fab-Antigen Complexes

Number PDB ID Description Resolution (Å) R-Free
1 1FE8 Von Willebrand factor A3 domain/Fab fragment of IGG RU5 that inhibits collagen binding 2.03 0.264
2 1FNS Von Willebrand factor A1 domain I546V mutant/the function blocking Fab NMC4 2 0.207
3 1H0D Human angiogenin/Fab of mAb 26-2F 2 0.272
4 1IQD Human factor VIII C2 domain/human monoclonal BO2C11 Fab. 2 0.253
5 1JPS Tissue factor/humanized Fab D3h44 1.85 0.224
6 1KB5 Murine T-cell variable domain/Fab 2.5 0.221
7 1LK3 Engineered human interleukin-10 monomer/9D7 Fab fragment 1.91 0.24
8 1MLC FAB D44.1/lysozyme 2.5 0.282
9 1OSP Outer surface protein A of borrelia burgdorferi/Fab of a murine mAb 1.95 0.295
10 1UJ3 A humanized Fab fragment of anti-tissue-factor antibody/tissue factor 2.1 0.227
11 1WEJ IgG1 Fab fragment (of E8 antibody)/horse cytochrome C 1.8 0.256
12 1YQV Fab HyHEL5/lysozyme 1.7 0.234
13 1ZTX West Nile virus envelope protein DIII/neutralizing E16 antibody Fab 2.5 0.282
14 2B2X VLA1 RdeltaH I-domain/a quadruple mutant of the AQC2 Fab 2.2 0.272
15 2CMR HIV-1 neutralizing antibody D5 Fab/the GP41 innter-core mimetic 5-helix 2 0.258
16 2DD8 SARS-CoV spike receptor-binding domain/neutralizing antibody 2.3 0.261
17 2FD6 Human urokinase plasminogen activator/urokinase receptor and an anti-upar antibody 1.9 0.276
18 2NXY HIV-1 gp120 envelope glycoprotein(S334A)/CD4 and antibody 17b 2 0.231
19 2Q8B Malaria antigen AMA1/growth-inhibitory antibody 2.3 0.256
20 2QQN Neuropilin-1 b1 Domain/VEGF-blocking Fab 2.2 0.207
21 2R0L Short form HGFA/Inhibitory Fab75 2.2 0.248
22 2VDR Integrin alphaIIBbetaA3 headpiece/a chimeric fibrinogen gamma chain peptide 2.4 0.193
23 3D85 Crystal structure of IL-23/neutralizing Fab 1.9 0.214
24 3D9A HyHel10 Fab/hen egg lysozyme 1.2 0.205
25 1BJ1 Vascular endothelial growth factor/neutralizing antibody 2.4 0.266
26 1CE1 Therapeutic antibody Fab/a synthetic peptide antigen 1.9 0.27
27 1N8Z Extracellular domain of human HER2/therapeutic Fab 2.52 0.284
28 1SY6 Crystal structure of CD3γε heterodimer/therapeutic Fab 2.1 0.255
29 1YY9 Extracellular domain of the epidermal growth factor receptor/neutralizing Fab 2.61 0.289

Our study is based on analysis of 29 Fab-antigen complex crystal structures (listed above) with resolution range 1.2–2.61 Å. All the Fabs in this study are different. This dataset compares favorably with the previous studies of Fab-antigen complex crystal structure data analyses (32,35,36). For example, Jackson et al. (1999) had studied 15 Fab-antigen complexes with resolution range 1.8–3.0 Å (32). The dataset of Lo Conte et al. (1999) contained 19 Fab-antigen complexes with resolution range 1.8–3.0 Å (35). The study of MacCallum et al. (1996) was based on 26 Fab-antigen complexes with 1.8–3.1 Å (36)