cryo-EM structure of Vitamin K-dependent gamma-carboxylase complexed with Matrix Gla protein. Determined by electron microscopy at 3.1 Å resolution. Released 22 Oct 2025.
Explore 9L24 in 3D Show helices and sheets RCSB PDB PDBe
9L24 contains 38 α-helices and 20 β-strands across 2 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 |
|---|---|---|---|
| α-helix | 43-45 | 3 | |
| α-helix | 48-55 | 8 | |
| β-strand | 59 | 1 | 1 |
| α-helix | 62-82 | 21 | |
| α-helix | 85-87 | 3 | |
| α-helix | 88-91 | 4 | |
| α-helix | 109-111 | 3 | |
| α-helix | 112-131 | 20 | |
| α-helix | 135-151 | 17 | |
| α-helix | 159-172 | 14 | |
| α-helix | 183-186 | 4 | |
| β-strand | 195 | 1 | 1 |
| α-helix | 198-217 | 20 | |
| α-helix | 221-224 | 4 | |
| α-helix | 232-234 | 3 | |
| α-helix | 236-238 | 3 | |
| α-helix | 239-242 | 4 | |
| α-helix | 247-250 | 4 | |
| α-helix | 251-258 | 8 | |
| α-helix | 259-271 | 13 | |
| α-helix | 276-293 | 18 | |
| α-helix | 299-305 | 7 | |
| α-helix | 307-310 | 4 | |
| α-helix | 315-322 | 8 | |
| α-helix | 325-327 | 3 | |
| α-helix | 332-333 | 2 | |
| α-helix | 336-339 | 4 | |
| α-helix | 360-376 | 17 | |
| α-helix | 377-379 | 3 | |
| α-helix | 385-387 | 3 | |
| β-strand | 406-417 | 12 | 2 |
| β-strand | 423-426 | 4 | 2 |
| α-helix | 436-438 | 3 | |
| α-helix | 441-454 | 14 | |
| α-helix | 455-458 | 4 | |
| β-strand | 463-473 | 11 | 2 |
| β-strand | 478 | 1 | 3 |
| β-strand | 479-480 | 2 | 2 |
| β-strand | 482 | 1 | 4 |
| β-strand | 502 | 1 | 4 |
| α-helix | 503-505 | 3 | |
| α-helix | 510-512 | 3 | |
| α-helix | 513-521 | 9 | |
| β-strand | 527-534 | 8 | 3 |
| β-strand | 539-543 | 5 | 5 |
| β-strand | 551 | 1 | 6 |
| β-strand | 552-557 | 6 | 3 |
| β-strand | 560-564 | 5 | 5 |
| β-strand | 569-573 | 5 | 5 |
| β-strand | 578 | 1 | 3 |
| β-strand | 581 | 1 | 6 |
| β-strand | 586-591 | 6 | 5 |
| β-strand | 597-604 | 8 | 3 |
| α-helix | 606-626 | 21 | |
| α-helix | 654-674 | 21 | |
| α-helix | 677-707 | 31 | |
| α-helix | 713-723 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 15-16 | 2 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Vitamin K-dependent gamma-carboxylase | A | protein | 698 | Homo sapiens | P38435 (AlphaFold model) |
| Matrix Gla protein | B | protein | 29 | Homo sapiens | P08493 (AlphaFold model) |
>9L24_1 Vitamin K-dependent gamma-carboxylase (chains A) SRIGKLLGFEWTDLSSWRRLVTLLNRPTDPASLAVFRFLFGFLMVLDIPQERGLSSLDRK YLDGLDVCRFPLLDALRPLPLDWMYLVYTIMFLGALGMMLGLCYRISCVLFLLPYWYVFL LDKTSWNNHSYLYGLLAFQLTFMDANHYWSVDGLLNAHRRNAHVPLWNYAVLRGQIFIVY FIAGVKKLDADWVEGYSMEYLSRHWLFSPFKLLLSEELTSLLVVHWGGLLLDLSAGFLLF FDVSRSIGLFFVSYFHCMNSQLFSIGMFSYVMLASSPLFCSPEWPRKLVSYCPRRLQQLL PLKAAPQPSVSCVYKRSRGKSGQKPGLRHQLGAAFTLLYLLEQLFLPYSHFLTQGYNNWT NGLYGYSWDMMVHSRSHQHVKITYRDGRTGELGYLNPGVFTQSRRWKDHADMLKQYATCL SRLLPKYNVTEPQIYFDIWVSINDRFQQRIFDPRVDIVQAAWSPFQRTSWVQPLLMDLSP WRAKLQEIKSSLDNHTEVVFIADFPGLHLENFVSEDLGNTSIQLLQGEVTVELVAEQKNQ TLREGEKMQLPAGEYHKVYTTSPSPSCYMYVYVNTTELALEQDLAYLQELKEKVENGSET GPLPPELQPLLEGEVKGGPEPTPLVQTFLRRQQRLQEIERRRNTPFHERFFRFLLRKLYV FRRSFLMTCISLRNLILGRPSLEQLAQEVTYANLRPFE
>9L24_2 Matrix Gla protein (chains B) LNPFINRRNANTFISPQQRWRAKVQERIR
| ID | Name | Formula | Copies |
|---|---|---|---|
| Y01 | Cholesterol hemisuccinate | C31 H50 O4 | 1 |
| PEE | 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine | C41 H78 N O8 P | 3 |
| CLR | Cholesterol | C27 H46 O | 1 |
| A1AVC | vitamin K1 hydroquinone | C31 H48 O2 | 1 |
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 1 |
Structural insight into bicarbonate-mediated carboxylation by human vitamin K-dependent carboxylase. Wu, K., Wang, Z., Yao, D. et al. Nat Commun (2025) 16:10480-10480. DOI 10.1038/s41467-025-65488-3 · PubMed
Other PDB entries of the same protein (UniProt P38435 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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