4HC1: Loop deleted mutant of human MAdCAM-1 D1D2
Crystal structure of a loop deleted mutant of human MAdCAM-1 D1D2 complexed with Fab 10G3. Determined by X-ray diffraction at 2.87 Å resolution. Released 23 Jan 2013.
- Method
- X-ray diffraction
- Resolution
- 2.87 Å
- Organisms
- Homo sapiens, Mus musculus
- Chains
- 6
- Atoms
- 9,648
- Mol. weight
- 138.36 kDa
- Ligands
- NAG
- Released
- 23 Jan 2013
Explore 4HC1 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
4HC1 contains 34 α-helices and 128 β-strands across 6 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.
Chain A: 1 helix, 20 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 12-16 | 5 | 1 |
| β-strand | 21-26 | 6 | 2 |
| β-strand | 35-38 | 4 | 1 |
| β-strand | 48-50 | 3 | 2 |
| β-strand | 54-59 | 6 | 2 |
| β-strand | 68-75 | 8 | 1 |
| β-strand | 80-90 | 11 | 1 |
| β-strand | 91 | 1 | 3 |
| β-strand | 96-99 | 4 | 4 |
| β-strand | 103 | 1 | 5 |
| β-strand | 109-117 | 9 | 4 |
| β-strand | 118 | 1 | 3 |
| β-strand | 125-131 | 7 | 6 |
| β-strand | 134-135 | 2 | 6 |
| β-strand | 141 | 1 | 4 |
| β-strand | 145-149 | 5 | 4 |
| β-strand | 160-168 | 9 | 4 |
| α-helix | 176-177 | 2 | |
| β-strand | 179-188 | 10 | 6 |
| β-strand | 191-200 | 10 | 6 |
| β-strand | 201 | 1 | 5 |
Chain B: 1 helix, 20 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 12-16 | 5 | 18 |
| β-strand | 21-26 | 6 | 19 |
| β-strand | 35-38 | 4 | 18 |
| β-strand | 48-50 | 3 | 19 |
| β-strand | 54-59 | 6 | 19 |
| β-strand | 68-75 | 8 | 18 |
| β-strand | 80-90 | 11 | 18 |
| β-strand | 91 | 1 | 20 |
| β-strand | 96-99 | 4 | 21 |
| β-strand | 103 | 1 | 22 |
| β-strand | 109-117 | 9 | 21 |
| β-strand | 118 | 1 | 20 |
| β-strand | 125-131 | 7 | 23 |
| β-strand | 134-135 | 2 | 23 |
| β-strand | 141 | 1 | 21 |
| β-strand | 145-151 | 7 | 21 |
| β-strand | 158-168 | 11 | 21 |
| α-helix | 176-177 | 2 | |
| β-strand | 179-188 | 10 | 23 |
| β-strand | 191-200 | 10 | 23 |
| β-strand | 201 | 1 | 22 |
Chains H and M: 9 helices, 23 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-7 | 5 | 7 |
| β-strand | 11-12 | 2 | 8 |
| β-strand | 18-25 | 8 | 7 |
| β-strand | 34-41 | 8 | 9 |
| β-strand | 45-53 | 9 | 9 |
| β-strand | 58-60 | 3 | 9 |
| α-helix | 62-64 | 3 | |
| β-strand | 68-69 | 2 | 7 |
| β-strand | 72-73 | 2 | 7 |
| β-strand | 78-83 | 6 | 7 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-99 | 8 | 9 |
| β-strand | 107-108 | 2 | 9 |
| β-strand | 112-114 | 3 | 9 |
| β-strand | 115-116 | 2 | 8 |
| α-helix | 119-121 | 3 | |
| β-strand | 122 | 1 | 10 |
| α-helix | 123-124 | 2 | |
| β-strand | 125-129 | 5 | 11 |
| α-helix | 130-132 | 3 | |
| β-strand | 140-150 | 11 | 11 |
| β-strand | 151 | 1 | 10 |
| β-strand | 156-159 | 4 | 12 |
| α-helix | 160-162 | 3 | |
| β-strand | 168-170 | 3 | 11 |
| α-helix | 171-173 | 3 | |
| β-strand | 174-176 | 3 | 11 |
| β-strand | 179-189 | 11 | 11 |
| β-strand | 199-204 | 6 | 12 |
| α-helix | 205-207 | 3 | |
| β-strand | 209-214 | 6 | 12 |
| α-helix | 215 | 1 | |
Chain L: 7 helices, 21 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-7 | 4 | 13 |
| β-strand | 10-14 | 5 | 14 |
| β-strand | 19-25 | 7 | 13 |
| β-strand | 33-38 | 6 | 14 |
| β-strand | 44-49 | 6 | 14 |
| β-strand | 53-54 | 2 | 14 |
| β-strand | 62-67 | 6 | 13 |
| β-strand | 70-75 | 6 | 13 |
| α-helix | 80-82 | 3 | |
| β-strand | 85-90 | 6 | 14 |
| α-helix | 96 | 1 | |
| β-strand | 97-98 | 2 | 14 |
| β-strand | 102-107 | 6 | 14 |
| β-strand | 111 | 1 | 15 |
| β-strand | 114-118 | 5 | 16 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-127 | 6 | |
| β-strand | 129-139 | 11 | 16 |
| β-strand | 140 | 1 | 15 |
| β-strand | 145-150 | 6 | 17 |
| β-strand | 153-155 | 3 | 17 |
| β-strand | 159-163 | 5 | 16 |
| α-helix | 164-167 | 4 | |
| β-strand | 173-182 | 10 | 16 |
| α-helix | 183-186 | 4 | |
| β-strand | 191-197 | 7 | 17 |
| α-helix | 204 | 1 | |
| β-strand | 205-210 | 6 | 17 |
Chain N: 7 helices, 21 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-7 | 4 | 30 |
| β-strand | 10-13 | 4 | 31 |
| β-strand | 18-25 | 8 | 30 |
| β-strand | 33-38 | 6 | 31 |
| β-strand | 44-49 | 6 | 31 |
| β-strand | 53-54 | 2 | 31 |
| β-strand | 62-67 | 6 | 30 |
| β-strand | 70-76 | 7 | 30 |
| α-helix | 80-82 | 3 | |
| β-strand | 85-90 | 6 | 31 |
| α-helix | 96 | 1 | |
| β-strand | 97-98 | 2 | 31 |
| β-strand | 102-106 | 5 | 31 |
| β-strand | 111 | 1 | 32 |
| β-strand | 114-118 | 5 | 33 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-127 | 6 | |
| β-strand | 129-139 | 11 | 33 |
| β-strand | 140 | 1 | 32 |
| β-strand | 145-150 | 6 | 34 |
| β-strand | 153-155 | 3 | 34 |
| β-strand | 159-163 | 5 | 33 |
| α-helix | 164-167 | 4 | |
| β-strand | 173-182 | 10 | 33 |
| α-helix | 183-186 | 4 | |
| β-strand | 191-197 | 7 | 34 |
| α-helix | 204 | 1 | |
| β-strand | 205-210 | 6 | 34 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Mucosal addressin cell adhesion molecule 1 | A, B | protein | 206 | Homo sapiens | Q13477 (AlphaFold model) |
| 10G3 heavy chain | H, M | protein | 220 | Mus musculus | |
| 10G3 light chain | L, N | protein | 214 | Mus musculus | |
Sequence of entity 1 (A, B), FASTA
>4HC1_1 Mucosal addressin cell adhesion molecule 1 (chains A, B)
VKPLQVEPPEPVVAVALGASRQLTCRLACADRGASVQWRGLDTSLGAVQSDTGRSVLTVR
NASLSAAGTRVCVGSCGGRTFQHTVQLLVYAFPNQLTVSPAALVPGDPEVACTAHKVTPV
DPNALSFSLLVGGQELEGAQALGPEVQQEPIGGDVLFRVTERWRLPPLGTPVPPALYCQA
TMRLPGLELSHRQAIPVLGGENLYFQ
Sequence of entity 2 (H, M), FASTA
>4HC1_2 10G3 heavy chain (chains H, M)
DVQLQESGPGLVKPSQSLSLTCSVTGYSITSGYYWNWIRQFPGNKLEWMGYISYDGSNNY
NPSLKNRVSITRDTSKNHFFLKLSSVTTEDTATYYCARASDSDGFAYWGQGTLVTVSAAK
TTAPSVYPLAPVCGGTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAILQSGLY
TLSSSVTVTSNTWPSQTITCNVAHPASSTKVDKKIEPRVP
Sequence of entity 3 (L, N), FASTA
>4HC1_3 10G3 light chain (chains L, N)
DILMTQSPSSMSVSLGDTVSFTCHASQGIGRNIGWLQQKPGKSFKGLIYHGTNLKDGVPS
RFSGSGSGADYSLTISRIESEDFADYYCIQYVQFPYTFGGGTKLEIKRADAAPTVSIFPP
SSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLT
LTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 2 |
Primary citation
A Different Fold with an Integrin-Binding Loop Specialized for Flexibility in Mucosal Addressin Cell Adhesion Molecule-1. Springer, T., Yu, Y., Zhu, J. et al. To be published.
Other PDB entries of the same protein (UniProt Q13477 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 4HBQ 1.4 Å, Crystal structure of a loop deleted mutant of Human MAdCAM-1 D1D2
- 4HD9 1.7 Å, Crystal structure of native human MAdCAM-1 D1D2 domain
- 1GSM 1.9 Å, A reassessment of the MAdCAM-1 structure and its role in integrin recognition.
- 1BQS 2.2 Å, The crystal structure of mucosal addressin cell adhesion molecule-1 (madcam-1)
- 4HCR 2.3 Å, Crystal structure of human MAdCAM-1 D1D2 complexed with Fab PF-547659
- 9P95 3.05 Å, CryoEM structure of integrin alpha4beta7 bound to MAdCAM-1
Browse structure collections
About this viewer
MolViewer shows 4HC1 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.