4UU9: Human c5a
Crystal structure of the human c5a in complex with MEDI7814 a neutralising antibody. Determined by X-ray diffraction at 2.12 Å resolution. Released 12 Aug 2015.
- Method
- X-ray diffraction
- Resolution
- 2.12 Å
- Organism
- HOMO SAPIENS
- Chains
- 6
- Atoms
- 4,778
- Mol. weight
- 67.41 kDa
- Released
- 12 Aug 2015
Explore 4UU9 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
4UU9 contains 27 α-helices and 48 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: 5 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-7 | 5 | 1 |
| β-strand | 11-12 | 2 | 2 |
| β-strand | 18-25 | 8 | 1 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 3 |
| β-strand | 45-51 | 7 | 3 |
| β-strand | 57-59 | 3 | 3 |
| α-helix | 61-63 | 3 | |
| β-strand | 67-72 | 6 | 1 |
| α-helix | 73-75 | 3 | |
| β-strand | 77-82 | 6 | 1 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-94 | 7 | 3 |
| α-helix | 98-100 | 3 | |
| β-strand | 102-103 | 2 | 3 |
| β-strand | 107-109 | 3 | 3 |
| β-strand | 110-111 | 2 | 2 |
Chain B: 4 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4 | 1 | 4 |
| β-strand | 5 | 1 | 5 |
| β-strand | 9-13 | 4 | 6 |
| β-strand | 19-24 | 6 | 5 |
| β-strand | 35-38 | 4 | 6 |
| β-strand | 45-46 | 2 | 6 |
| α-helix | 47-50 | 4 | |
| α-helix | 53-54 | 2 | |
| α-helix | 58-60 | 3 | |
| β-strand | 62-67 | 6 | 5 |
| β-strand | 70-75 | 6 | 5 |
| α-helix | 80-82 | 3 | |
| β-strand | 84-88 | 5 | 6 |
| β-strand | 89-92 | 4 | 7 |
| β-strand | 95A-98 | 4 | 7 |
| β-strand | 99 | 1 | 4 |
| β-strand | 102-106 | 5 | 6 |
Chain C: 4 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 1-10 | 10 | |
| α-helix | 16-26 | 11 | |
| α-helix | 34-38 | 5 | |
| α-helix | 45-63 | 19 | |
Chain D: 4 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 1-10 | 10 | |
| α-helix | 16-26 | 11 | |
| α-helix | 34-38 | 5 | |
| α-helix | 45-64 | 20 | |
Chain H: 5 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-7 | 5 | 8 |
| β-strand | 10-12 | 3 | 9 |
| β-strand | 18-25 | 8 | 8 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 9 |
| β-strand | 45-51 | 7 | 9 |
| β-strand | 57-59 | 3 | 9 |
| β-strand | 67-72 | 6 | 8 |
| α-helix | 73-75 | 3 | |
| β-strand | 77-82 | 6 | 8 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-94 | 7 | 9 |
| α-helix | 95-97 | 3 | |
| α-helix | 98-100 | 3 | |
| β-strand | 102-103 | 2 | 9 |
| β-strand | 107-111 | 5 | 9 |
Chain L: 5 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4 | 1 | 10 |
| β-strand | 5 | 1 | 11 |
| β-strand | 9-13 | 4 | 12 |
| β-strand | 19-24 | 6 | 11 |
| α-helix | 27C-29 | 3 | |
| β-strand | 34-38 | 5 | 12 |
| β-strand | 45-46 | 2 | 12 |
| α-helix | 47-50 | 4 | |
| α-helix | 53-54 | 2 | |
| α-helix | 58-60 | 3 | |
| β-strand | 62-67 | 6 | 11 |
| β-strand | 70-75 | 6 | 11 |
| α-helix | 80-82 | 3 | |
| β-strand | 84-92 | 9 | 12 |
| β-strand | 95A-98 | 4 | 12 |
| β-strand | 99 | 1 | 10 |
| β-strand | 102-106 | 5 | 12 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| MEDI7814 | A, H | protein | 123 | HOMO SAPIENS | |
| MEDI7814 | B, L | protein | 111 | HOMO SAPIENS | |
| Complement C5 | C, D | protein | 75 | HOMO SAPIENS | P01031 (AlphaFold model) |
Sequence of entity 1 (A, H), FASTA
>4UU9_1 MEDI7814 (chains A, H)
EVQLLESGGGLVQPGGSLRLSCAASGFTFSSYAMSWVRQAPGKGLEWVSAISGSGGSTYY
ADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCARDDDYEEWPWYYGMDVWGQGTMV
TVS
Sequence of entity 2 (B, L), FASTA
>4UU9_2 MEDI7814 (chains B, L)
QSALTQPASVSGSPGQSITISCTGTSSDIGGSKYVSWYQQHPGKAPKLIIFDVNRRPSGL
SNRFSASKSGNTASLTISGLQAEDEADYYCTSYHPTKTILFGGGTKLTVLA
Sequence of entity 3 (C, D), FASTA
>4UU9_3 COMPLEMENT C5 (chains C, D)
STLQKKIEEIAAKYKHSVVKKCCYDGACVNNDETCEQRAARISLGPRCIKAFTECCVVAS
QLRANISHKDMQLGR
Primary citation
Structure and characterization of a high affinity C5a monoclonal antibody that blocks binding to C5aR1 and C5aR2 receptors. Colley, C.S., Popovic, B., Sridharan, S. et al. MAbs (2018) 10:104-117. DOI 10.1080/19420862.2017.1384892 · PubMed
Other PDB entries of the same protein (UniProt P01031 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 9Y6C 2.0 Å, X-ray structure analysis of human Complement Component 5 TE domain in complex with the…
- 5B71 2.11 Å, Crystal structure of complement C5 in complex with SKY59
- 7AD7 2.3 Å, Crystal structure of human complement C5 in complex with the K8 bovine knob domain…
- 5B4P 2.4 Å, Complex structure of human C5a and its binding repebody
- 4P39 2.4 Å, Crystal structure of the human C5aR antagonist C5a-A8
- 7OP0 2.57 Å, Crystal structure of complement C5 in complex with chemically synthesized K92 knob domain.
- 3HQA 2.59 Å, Crystal structure of human desarg-C5A
- 5HCC 2.59 Å, Ternary complex of human Complement C5 with Ornithodoros moubata OmCI and Dermacentor…
- 22GM 2.7 Å, C5a bound C5aR1 in complex with beta-arrestin1
- 6RPT 2.7 Å, Structure of tick complement inhibitor CirpT1 complexed with macroglobubulin domain 4 of…
- 7AD6 2.75 Å, Crystal structure of human complement C5 in complex with the K92 bovine knob domain…
- 22GK 2.84 Å, C5a bound C5aR2 in complex with beta-arrestin1
Browse structure collections
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