3EO1: Fab Fragment of GC-1008
Structure of the Fab Fragment of GC-1008 in Complex with Transforming Growth Factor-Beta 3. Determined by X-ray diffraction at 3.1 Å resolution. Released 2 Dec 2008.
- Method
- X-ray diffraction
- Resolution
- 3.1 Å
- Organisms
- Mus musculus, Homo sapiens
- Chains
- 12
- Atoms
- 16,556
- Mol. weight
- 240 kDa
- Released
- 2 Dec 2008
Explore 3EO1 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
3EO1 contains 64 α-helices and 220 β-strands across 12 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
Chains A and G: 6 helices, 21 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-7 | 4 | 1 |
| β-strand | 10-13 | 4 | 2 |
| α-helix | 18 | 1 | |
| β-strand | 19-29 | 11 | 1 |
| β-strand | 34-39 | 6 | 2 |
| β-strand | 46-51 | 6 | 2 |
| β-strand | 54-55 | 2 | 2 |
| β-strand | 63-76 | 14 | 1 |
| α-helix | 81-83 | 3 | |
| β-strand | 86-91 | 6 | 2 |
| β-strand | 94 | 1 | 3 |
| α-helix | 97 | 1 | |
| β-strand | 98-99 | 2 | 2 |
| β-strand | 104-107 | 4 | 2 |
| β-strand | 112 | 1 | 4 |
| β-strand | 116-118 | 3 | 5 |
| α-helix | 120-122 | 3 | |
| α-helix | 123-126 | 4 | |
| β-strand | 132-140 | 9 | 5 |
| β-strand | 141 | 1 | 4 |
| β-strand | 146-151 | 6 | 6 |
| β-strand | 161-164 | 4 | 5 |
| β-strand | 174-181 | 8 | 5 |
| α-helix | 184-187 | 4 | |
| β-strand | 193-198 | 6 | 6 |
| β-strand | 206 | 1 | 6 |
| β-strand | 209-210 | 2 | 6 |
Chains B and H: 2 helices, 21 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-6 | 3 | 7 |
| β-strand | 10-12 | 3 | 8 |
| β-strand | 18-24 | 7 | 7 |
| β-strand | 34-39 | 6 | 8 |
| β-strand | 45-52 | 8 | 8 |
| β-strand | 57-60 | 4 | 8 |
| α-helix | 62-64 | 3 | |
| β-strand | 68-73 | 6 | 7 |
| β-strand | 78-83 | 6 | 7 |
| β-strand | 92-99 | 8 | 8 |
| β-strand | 107-110 | 4 | 8 |
| β-strand | 115-118 | 4 | 8 |
| β-strand | 128-131 | 4 | 9 |
| β-strand | 142-149 | 8 | 9 |
| β-strand | 152 | 1 | 10 |
| β-strand | 157-158 | 2 | 11 |
| β-strand | 170-172 | 3 | 9 |
| α-helix | 173-175 | 3 | |
| β-strand | 176-177 | 2 | 10 |
| β-strand | 183-184 | 2 | 10 |
| β-strand | 187-192 | 6 | 9 |
| β-strand | 203-207 | 5 | 11 |
| β-strand | 212-216 | 5 | 11 |
Chains C and I: 5 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-3 | 2 | 12 |
| α-helix | 4-7 | 4 | |
| β-strand | 16-18 | 3 | 13 |
| β-strand | 22-23 | 2 | 14 |
| α-helix | 24-28 | 5 | |
| β-strand | 33-35 | 3 | 12 |
| β-strand | 38-39 | 2 | 14 |
| β-strand | 43-45 | 3 | 13 |
| β-strand | 54 | 1 | 12 |
| α-helix | 57-68 | 12 | |
| α-helix | 70-72 | 3 | |
| α-helix | 75-77 | 3 | |
| β-strand | 78-91 | 14 | 12 |
| β-strand | 93 | 1 | 3 |
| β-strand | 96-111 | 16 | 12 |
Chains D and J: 8 helices, 27 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 6-7 | 2 | 15 |
| β-strand | 10 | 1 | 16 |
| β-strand | 13 | 1 | 17 |
| α-helix | 18 | 1 | |
| β-strand | 19-23 | 5 | 15 |
| β-strand | 34-39 | 6 | 16 |
| β-strand | 46-49 | 4 | 16 |
| β-strand | 55 | 1 | 16 |
| α-helix | 56 | 1 | |
| β-strand | 63-64 | 2 | 15 |
| β-strand | 67-68 | 2 | 15 |
| β-strand | 71-76 | 6 | 15 |
| α-helix | 81-83 | 3 | |
| β-strand | 86-91 | 6 | 16 |
| α-helix | 97 | 1 | |
| β-strand | 98-99 | 2 | 16 |
| β-strand | 103-104 | 2 | 16 |
| α-helix | 106 | 1 | |
| β-strand | 107 | 1 | 17 |
| α-helix | 108 | 1 | |
| β-strand | 112 | 1 | 18 |
| β-strand | 117-118 | 2 | 19 |
| β-strand | 132-134 | 3 | 20 |
| β-strand | 135-136 | 2 | 19 |
| β-strand | 140 | 1 | 21 |
| β-strand | 141 | 1 | 18 |
| β-strand | 145-148 | 4 | 22 |
| β-strand | 151 | 1 | 22 |
| β-strand | 161-164 | 4 | 20 |
| α-helix | 165-168 | 4 | |
| β-strand | 174 | 1 | 21 |
| β-strand | 176-181 | 6 | 20 |
| α-helix | 184-187 | 4 | |
| β-strand | 192-199 | 8 | 22 |
| β-strand | 207-211 | 5 | 22 |
Chains E and K: 5 helices, 22 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-6 | 3 | 23 |
| α-helix | 7-9 | 3 | |
| β-strand | 10-12 | 3 | 24 |
| β-strand | 18-24 | 7 | 23 |
| β-strand | 34-39 | 6 | 24 |
| β-strand | 45-52 | 8 | 24 |
| β-strand | 57-60 | 4 | 24 |
| α-helix | 62-64 | 3 | |
| β-strand | 68 | 1 | 23 |
| β-strand | 71 | 1 | 23 |
| β-strand | 78-83 | 6 | 23 |
| β-strand | 92-98 | 7 | 24 |
| β-strand | 109-110 | 2 | 24 |
| β-strand | 115-118 | 4 | 24 |
| β-strand | 124 | 1 | 25 |
| β-strand | 127-131 | 5 | 26 |
| β-strand | 144-152 | 9 | 26 |
| β-strand | 153 | 1 | 25 |
| β-strand | 158-159 | 2 | 27 |
| α-helix | 162-164 | 3 | |
| β-strand | 171-172 | 2 | 26 |
| α-helix | 173-175 | 3 | |
| β-strand | 177 | 1 | 26 |
| β-strand | 183-190 | 8 | 26 |
| α-helix | 193-195 | 3 | |
| β-strand | 205-207 | 3 | 27 |
| β-strand | 212-214 | 3 | 27 |
Chains F and L: 6 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-3 | 2 | 28 |
| α-helix | 4-7 | 4 | |
| β-strand | 16-18 | 3 | 29 |
| α-helix | 19 | 1 | |
| β-strand | 21-23 | 3 | 30 |
| α-helix | 24-28 | 5 | |
| β-strand | 35 | 1 | 28 |
| β-strand | 38-40 | 3 | 30 |
| β-strand | 43-45 | 3 | 29 |
| β-strand | 54 | 1 | 28 |
| α-helix | 57-68 | 12 | |
| α-helix | 70-72 | 3 | |
| α-helix | 75-77 | 3 | |
| β-strand | 78-92 | 15 | 28 |
| β-strand | 95-111 | 17 | 28 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| GC-1008 Fab Light Chain | A, D, G, J | protein | 215 | Mus musculus | Q6PJF2 (AlphaFold model) |
| GC-1008 Fab Heavy Chain | B, E, H, K | protein | 225 | Mus musculus | P01861 (AlphaFold model) |
| Transforming growth factor beta-3 | C, F, I, L | protein | 112 | Homo sapiens | P10600 (AlphaFold model) |
Sequence of entity 1 (A, D, G, J), FASTA
>3EO1_1 GC-1008 Fab Light Chain (chains A, D, G, J)
ETVLTQSPGTLSLSPGERATLSCRASQSLGSSYLAWYQQKPGQAPRLLIYGASSRAPGIP
DRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYADSPITFGQGTRLEIKRTVAAPSVFIFP
PSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTL
TLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
Sequence of entity 2 (B, E, H, K), FASTA
>3EO1_2 GC-1008 Fab Heavy Chain (chains B, E, H, K)
QVQLVQSGAEVKKPGSSVKVSCKASGYTFSSNVISWVRQAPGQGLEWMGGVIPIVDIANY
AQRFKGRVTITADESTSTTYMELSSLRSEDTAVYYCASTLGLVLDAMDYWGQGTLVTVSS
ASTKGPSVFPLAPCSRSTSESTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSS
GLYSLSSVVTVPSSSLGTKTYTCNVDHKPSNTKVDKRVESKYGPP
Sequence of entity 3 (C, F, I, L), FASTA
>3EO1_3 Transforming growth factor beta-3 (chains C, F, I, L)
ALDTNYCFRNLEENCCVRPLYIDFRQDLGWKWVHEPKGYYANFCSGPCPYLRSADTTHST
VLGLYNTLNPEASASPCCVPQDLEPLTILYYVGRTPKVEQLSNMVVKSCKCS
Primary citation
A cytokine-neutralizing antibody as a structural mimetic of 2 receptor interactions. Wilkinson, T., Turner, R., Podichetty, S. et al. Proc Natl Acad Sci U S A (2008) 105:20251-20256. DOI 10.1073/pnas.0807200106 · PubMed
Other PDB entries of the same protein (UniProt Q6PJF2 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 3EO0 1.75 Å, Structure of the Transforming Growth Factor-Beta Neutralizing Antibody GC-1008
- 8QH0 1.87 Å, Crystal structure of the SARS-CoV-2 RBD with the antibody Cv2.3194
- 1DN0 2.28 Å, Structure of the FAB fragment from a human IgM cold agglutinin
- 2AGJ 2.6 Å, Crystal Structure of a glycosylated Fab from an IgM cryoglobulin with properties of a…
- 8QH1 2.65 Å, Crystal structure of the SARS-CoV-2 RBD from the Omicron BA4 variant with the antibody…
- 1U6A 2.81 Å, Crystal Structure of the Broadly Neutralizing Anti-HIV Fab F105
- 1QLR 2.83 Å, Crystal structure of the FAB fragment of a human monoclonal IgM cold agglutinin
- 4YPG 3.0 Å, Structural Insights Into the Neutralization Properties of a Human Anti-Interferon…
- 3B2V 3.3 Å, Crystal structure of the extracellular region of the epidermal growth factor receptor in…
- 6MYY 3.8 Å, Germline VRC01 antibody recognition of a modified clade C HIV-1 envelope trimer, 3 Fabs…
- 6UDK 3.9 Å, HIV-1 bNAb 1-55 in complex with modified BG505 SOSIP-based immunogen RC1 and 10-1074
- 6MZJ 4.8 Å, Germline VRC01 antibody recognition of a modified clade C HIV-1 envelope trimer, 2 Fabs…
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