The crystal structure of human MACROD2 in space group P43212. Determined by X-ray diffraction at 1.9 Å resolution. Released 30 Sept 2020.
Explore 6Y4Z in 3D Show helices and sheets RCSB PDB PDBe
6Y4Z contains 54 α-helices and 36 β-strands across 4 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 | 8-19 | 12 | |
| α-helix | 23-28 | 6 | |
| β-strand | 35-36 | 2 | 1 |
| α-helix | 37-39 | 3 | |
| α-helix | 41-42 | 2 | |
| α-helix | 43-48 | 6 | |
| α-helix | 68-70 | 3 | |
| β-strand | 72-75 | 4 | 2 |
| α-helix | 79-81 | 3 | |
| β-strand | 82-83 | 2 | 1 |
| β-strand | 86-91 | 6 | 2 |
| α-helix | 100-109 | 10 | |
| α-helix | 111-119 | 9 | |
| β-strand | 125 | 1 | 2 |
| β-strand | 128-132 | 5 | 2 |
| β-strand | 140-145 | 6 | 2 |
| α-helix | 155-174 | 20 | |
| β-strand | 179-182 | 4 | 2 |
| α-helix | 188-190 | 3 | |
| α-helix | 194-212 | 19 | |
| α-helix | 213-215 | 3 | |
| β-strand | 218-222 | 5 | 2 |
| α-helix | 226-240 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 11-19 | 9 | |
| α-helix | 23-29 | 7 | |
| β-strand | 35-36 | 2 | 3 |
| α-helix | 37-39 | 3 | |
| α-helix | 41-42 | 2 | |
| α-helix | 43-46 | 4 | |
| α-helix | 68-70 | 3 | |
| β-strand | 72-76 | 5 | 4 |
| α-helix | 79-81 | 3 | |
| β-strand | 82-83 | 2 | 3 |
| β-strand | 86-91 | 6 | 4 |
| α-helix | 100-109 | 10 | |
| α-helix | 111-118 | 8 | |
| β-strand | 125 | 1 | 4 |
| β-strand | 128-132 | 5 | 4 |
| β-strand | 140-145 | 6 | 4 |
| α-helix | 155-174 | 20 | |
| β-strand | 179-182 | 4 | 4 |
| α-helix | 188-190 | 3 | |
| α-helix | 194-212 | 19 | |
| α-helix | 213-215 | 3 | |
| β-strand | 218-223 | 6 | 4 |
| α-helix | 226-240 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 11-19 | 9 | |
| α-helix | 23-27 | 5 | |
| β-strand | 35-36 | 2 | 5 |
| α-helix | 37-39 | 3 | |
| α-helix | 43-47 | 5 | |
| α-helix | 68-70 | 3 | |
| β-strand | 72-76 | 5 | 6 |
| α-helix | 79-81 | 3 | |
| β-strand | 82-83 | 2 | 5 |
| β-strand | 86-91 | 6 | 6 |
| α-helix | 100-109 | 10 | |
| α-helix | 111-119 | 9 | |
| β-strand | 125 | 1 | 6 |
| β-strand | 128-132 | 5 | 6 |
| β-strand | 140-145 | 6 | 6 |
| α-helix | 155-174 | 20 | |
| β-strand | 179-182 | 4 | 6 |
| α-helix | 188-190 | 3 | |
| α-helix | 194-212 | 19 | |
| α-helix | 213-215 | 3 | |
| β-strand | 218-223 | 6 | 6 |
| α-helix | 226-239 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 11-20 | 10 | |
| α-helix | 23-27 | 5 | |
| β-strand | 35-36 | 2 | 7 |
| α-helix | 37-39 | 3 | |
| α-helix | 43-47 | 5 | |
| α-helix | 68-70 | 3 | |
| β-strand | 72-76 | 5 | 8 |
| α-helix | 79-81 | 3 | |
| β-strand | 82-83 | 2 | 7 |
| β-strand | 86-91 | 6 | 8 |
| α-helix | 100-109 | 10 | |
| α-helix | 111-118 | 8 | |
| β-strand | 125 | 1 | 8 |
| β-strand | 128-132 | 5 | 8 |
| β-strand | 140-145 | 6 | 8 |
| α-helix | 155-174 | 20 | |
| β-strand | 179-182 | 4 | 8 |
| α-helix | 188-190 | 3 | |
| α-helix | 194-212 | 19 | |
| α-helix | 213-215 | 3 | |
| β-strand | 218-223 | 6 | 8 |
| α-helix | 226-239 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Thioredoxin 1,ADP-ribose glycohydrolase MACROD2 | A, B, C, D | protein | 366 | Escherichia coli (strain K12), Homo sapiens | A1Z1Q3 (AlphaFold model), P0AA25 (AlphaFold model) |
>6Y4Z_1 Thioredoxin 1,ADP-ribose glycohydrolase MACROD2 (chains A, B, C, D) MHHHHHHSSGMSDKIIHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPILDEIADEY QGKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKNGEVAATKVGALSKGQLKEFLDANLAG TENLYFQSMKKKVWREEKERLLKMTLEERRKEYLRDYIPLNSILSWKEEMKGKGQNDEEN TQETSQVKKSLTEKVSLYRGDITLLEVDAIVNAANASLLGGGGVDGCIHRAAGPCLLAEC RNLNGCDTGHAKITCGYDLPAKYVIHTVGPIARGHINGSHKEDLANCYKSSLKLVKENNI RSVAFPCISTGIYGFPNEPAAVIALNTIKEWLAKNHHEVDRIIFCVFLEVDFKIYKKKMN EFFSVD
| ID | Name | Formula | Copies |
|---|---|---|---|
| TLA | L(+)-tartaric acid | C4 H6 O6 | 1 |
Multiple crystal forms of human MacroD2. Wazir, S., Maksimainen, M.M., Lehtio, L. Acta Crystallogr F Struct Biol Commun (2020) 76:477-482. DOI 10.1107/S2053230X20011309 · PubMed
Other PDB entries of the same protein (UniProt A1Z1Q3 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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