Catalytic fragment of MASP-2 in complex with its specific inhibitor developed by directed evolution on SGCI scaffold. Determined by X-ray diffraction at 1.28 Å resolution. Released 25 Apr 2012.
Explore 3TVJ in 3D Show helices and sheets RCSB PDB PDBe
3TVJ contains 18 α-helices and 32 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 | 365 | 1 | 1 |
| α-helix | 369-371 | 3 | |
| β-strand | 375-379 | 5 | 2 |
| β-strand | 387 | 1 | 1 |
| β-strand | 391-396 | 6 | 2 |
| α-helix | 397 | 1 | |
| β-strand | 401-404 | 4 | 3 |
| β-strand | 409-412 | 4 | 2 |
| β-strand | 418-420 | 3 | 2 |
| α-helix | 427-428 | 2 | |
| β-strand | 429-432 | 4 | 3 |
| α-helix | 433-434 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 446 | 1 | 4 |
| β-strand | 449-450 | 2 | 5 |
| α-helix | 451-452 | 2 | |
| β-strand | 459-463 | 5 | 6 |
| β-strand | 466-472 | 7 | 6 |
| β-strand | 477-480 | 4 | 6 |
| α-helix | 482-485 | 4 | |
| α-helix | 486-490 | 5 | |
| α-helix | 494-495 | 2 | |
| β-strand | 496-499 | 4 | 6 |
| β-strand | 503 | 1 | 7 |
| α-helix | 509 | 1 | |
| β-strand | 510-519 | 10 | 6 |
| β-strand | 534-538 | 5 | 6 |
| α-helix | 541-544 | 4 | |
| β-strand | 545 | 1 | 8 |
| β-strand | 548 | 1 | 8 |
| α-helix | 550-551 | 2 | |
| β-strand | 552 | 1 | 5 |
| α-helix | 553-554 | 2 | |
| α-helix | 558-561 | 4 | |
| β-strand | 567-572 | 6 | 5 |
| β-strand | 584 | 1 | 7 |
| β-strand | 586-592 | 7 | 5 |
| α-helix | 593-594 | 2 | |
| α-helix | 595-603 | 9 | |
| α-helix | 608 | 1 | |
| β-strand | 616-619 | 4 | 5 |
| β-strand | 627 | 1 | 4 |
| β-strand | 636-641 | 6 | 5 |
| β-strand | 646-657 | 12 | 5 |
| β-strand | 667-671 | 5 | 5 |
| α-helix | 672-675 | 4 | |
| α-helix | 676-685 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 9-12 | 4 | 5 |
| β-strand | 15-19 | 5 | 5 |
| β-strand | 26-29 | 4 | 5 |
| β-strand | 32-33 | 2 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Mannan-binding lectin serine protease 2 A chain | A | protein | 86 | Homo sapiens | O00187 (AlphaFold model) |
| Mannan-binding lectin serine protease 2 B chain | B | protein | 242 | Homo sapiens | O00187 (AlphaFold model) |
| Protease inhibitor SGPI-2 | I | protein | 38 | Schistocerca gregaria | O46162 (AlphaFold model) |
>3TVJ_1 Mannan-binding lectin serine protease 2 A chain (chains A) ASMTIVDCGPPDDLPSGRVEYITGPGVTTYKAVIQYSCEETFYTMKVNDGKYVCDADGFW TSSKGEKSLPVCEPVCGLSARTTGGR
>3TVJ_2 Mannan-binding lectin serine protease 2 B chain (chains B) IYGGQKAKPGDFPWQVLILGGTTAAGALLYDNWVLTAAHAVYEQKHDASALDIRMGTLKR LSPHYTQAWSEAVFIHEGYTHDAGFDNDIALIKLNNKVVINSNITPICLPRKEAESFMRT DDIGTASGWGLTQRGFLARNLMYVDIPIVDHQKCTAAYEKPPYPRGSVTANMLCAGLESG GKDSCRGDSGGALVFLDSETERWFVGGIVSWGSMNCGEAGQYGVYTKVINYIPWIENIIS DF
>3TVJ_3 Protease inhibitor SGPI-2 (chains I) GSGEVTCEPGTTFKDKCNTCRCGSDGKSAVCTKLWCNQ
Monospecific Inhibitors Show That Both Mannan-binding Lectin-associated Serine Protease-1 (MASP-1) and -2 Are Essential for Lectin Pathway Activation and Reveal Structural Plasticity of MASP-2. Heja, D., Harmat, V., Fodor, K. et al. J Biol Chem (2012) 287:20290-20300. DOI 10.1074/jbc.M112.354332 · PubMed
Other PDB entries of the same protein (UniProt O00187 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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