Crystal structure of HLA-C*14:02 complexed with KIR2DL2. Determined by X-ray diffraction at 2.5 Å resolution. Released 24 Dec 2025.
Explore 9L4I in 3D Show helices and sheets RCSB PDB PDBe
9L4I contains 16 α-helices and 52 β-strands across 3 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-12 | 9 | 1 |
| α-helix | 20 | 1 | |
| β-strand | 21-28 | 8 | 1 |
| β-strand | 31-37 | 7 | 1 |
| β-strand | 46-47 | 2 | 1 |
| α-helix | 50-52 | 3 | |
| α-helix | 57-84 | 28 | |
| β-strand | 94-103 | 10 | 1 |
| β-strand | 109-118 | 10 | 1 |
| β-strand | 121-126 | 6 | 1 |
| β-strand | 133-135 | 3 | 1 |
| α-helix | 138-149 | 12 | |
| α-helix | 152-158 | 7 | |
| α-helix | 159-163 | 5 | |
| α-helix | 164-174 | 11 | |
| α-helix | 176-179 | 4 | |
| β-strand | 183 | 1 | 2 |
| α-helix | 184-185 | 2 | |
| β-strand | 186-192 | 7 | 3 |
| β-strand | 199-208 | 10 | 3 |
| β-strand | 209 | 1 | 2 |
| β-strand | 214-219 | 6 | 4 |
| β-strand | 222-223 | 2 | 4 |
| α-helix | 225-227 | 3 | |
| β-strand | 228-230 | 3 | 3 |
| α-helix | 231-233 | 3 | |
| β-strand | 234-235 | 2 | 3 |
| β-strand | 241-249 | 9 | 3 |
| α-helix | 254-256 | 3 | |
| β-strand | 257-262 | 6 | 4 |
| β-strand | 270-272 | 3 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3 | 1 | 5 |
| α-helix | 4-5 | 2 | |
| β-strand | 6-11 | 6 | 6 |
| β-strand | 21-30 | 10 | 6 |
| β-strand | 31 | 1 | 5 |
| β-strand | 36-41 | 6 | 7 |
| β-strand | 44-45 | 2 | 7 |
| β-strand | 50-51 | 2 | 6 |
| β-strand | 55-56 | 2 | 6 |
| β-strand | 62-70 | 9 | 6 |
| β-strand | 78-83 | 6 | 7 |
| β-strand | 91-94 | 4 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 9-13 | 5 | 8 |
| β-strand | 17-19 | 3 | 9 |
| β-strand | 24-30 | 7 | 8 |
| β-strand | 36-42 | 7 | 10 |
| β-strand | 47-52 | 6 | 10 |
| β-strand | 54 | 1 | 8 |
| β-strand | 60-66 | 7 | 8 |
| α-helix | 71-73 | 3 | |
| β-strand | 75-82 | 8 | 10 |
| β-strand | 90 | 1 | 10 |
| α-helix | 92-96 | 5 | |
| β-strand | 97-99 | 3 | 10 |
| β-strand | 100-102 | 3 | 9 |
| β-strand | 109-112 | 4 | 11 |
| β-strand | 117-118 | 2 | 12 |
| β-strand | 123-130 | 8 | 11 |
| β-strand | 136-140 | 5 | 13 |
| β-strand | 148-151 | 4 | 13 |
| β-strand | 160-168 | 9 | 11 |
| β-strand | 174-175 | 2 | 14 |
| β-strand | 176-181 | 6 | 13 |
| β-strand | 184-188 | 5 | 13 |
| α-helix | 190-194 | 5 | |
| β-strand | 195-196 | 2 | 14 |
| β-strand | 198-199 | 2 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| MHC class I antigen | A | protein | 273 | Homo sapiens | G9MDC7 (AlphaFold model) |
| Beta-2-microglobulin | B | protein | 100 | Homo sapiens | P61769 (AlphaFold model) |
| LL8 | C | protein | 8 | Homo sapiens | |
| Killer cell immunoglobulin-like receptor 2DL2 | D | protein | 196 | Homo sapiens | P43627 (AlphaFold model) |
>9L4I_1 MHC class I antigen (chains A) SHSMRYFSTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASPRGEPRAPWVEQEGPEYWD RETQKYKRQAQTDRVSLRNLRGYYNQSEAGSHTLQWMFGCDLGPDGRLLRGYDQSAYDGK DYIALNEDLRSWTAADTAAQITQRKWEAAREAEQRRAYLEGTCVEWLRRYLENGKETLQR AEHPKTHVTHHPVSDHEATLRCWALGFYPAEITLTWQWDGEDQTQDTELVETRPAGDGTF QKWAAVVVPSGEEQRYTCHVQHEGLPEPLTLRW
>9L4I_2 Beta-2-microglobulin (chains B) MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKD WSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM
>9L4I_3 LL8 (chains C) LYNTVATL
>9L4I_4 Killer cell immunoglobulin-like receptor 2DL2 (chains D) HRKPSLLAHPGRLVKSEETVILQCWSDVRFEHFLLHREGKFKDTLHLIGEHHDGVSKANF SIGPMMQDLAGTYRCYGSVTHSPYQLSAPSDPLDIVITGLYEKPSLSAQPGPTVLAGESV TLSCSSRSSYDMYHLSLEGEAHECRFSAGPKVNGTFQADFPLGPATHGGTYRCFGSFRDS PYEWSNSSDPLLVSVI
Micropolymorphism outside the peptide-binding groove of human leukocyte antigen (HLA)-C*14 modulates structural stability and shapes immune responses. Liu, Q., Yang, M., Zhong, P. et al. Int J Biol Macromol (2025) 309:142772-142772. DOI 10.1016/j.ijbiomac.2025.142772 · PubMed
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