Crystal Structure of the Catalytic Core of CBP. Determined by X-ray diffraction at 2.4 Å resolution. Released 21 Jun 2017.
Explore 5U7G in 3D Show helices and sheets RCSB PDB PDBe
5U7G contains 64 α-helices and 32 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 | 1088-1103 | 16 | |
| α-helix | 1110-1112 | 3 | |
| α-helix | 1118-1121 | 4 | |
| α-helix | 1126-1129 | 4 | |
| α-helix | 1136-1145 | 10 | |
| α-helix | 1151-1168 | 18 | |
| α-helix | 1174-1196 | 23 | |
| β-strand | 1206 | 1 | 1 |
| α-helix | 1277 | 1 | |
| β-strand | 1278 | 1 | 1 |
| α-helix | 1279-1280 | 2 | |
| β-strand | 1281-1283 | 3 | 2 |
| β-strand | 1290-1292 | 3 | 2 |
| α-helix | 1293-1296 | 4 | |
| α-helix | 1310-1314 | 5 | |
| α-helix | 1320-1322 | 3 | |
| α-helix | 1331-1332 | 2 | |
| α-helix | 1334-1350 | 17 | |
| β-strand | 1358-1371 | 14 | 3 |
| α-helix | 1372-1373 | 2 | |
| α-helix | 1374-1376 | 3 | |
| α-helix | 1377-1381 | 5 | |
| β-strand | 1389-1403 | 15 | 3 |
| β-strand | 1406-1418 | 13 | 3 |
| α-helix | 1423 | 1 | |
| β-strand | 1429-1437 | 9 | 3 |
| α-helix | 1444-1446 | 3 | |
| α-helix | 1447-1465 | 19 | |
| β-strand | 1469-1473 | 5 | 3 |
| α-helix | 1497-1513 | 17 | |
| β-strand | 1519-1522 | 4 | 3 |
| α-helix | 1523-1530 | 8 | |
| α-helix | 1535-1537 | 3 | |
| α-helix | 1545-1555 | 11 | |
| α-helix | 1622-1628 | 7 | |
| α-helix | 1630-1632 | 3 | |
| β-strand | 1633-1637 | 5 | 3 |
| α-helix | 1648-1650 | 3 | |
| α-helix | 1655-1656 | 2 | |
| α-helix | 1660-1662 | 3 | |
| α-helix | 1666-1675 | 10 | |
| α-helix | 1682-1699 | 18 | |
| β-strand | 1707 | 1 | 4 |
| β-strand | 1714 | 1 | 4 |
| β-strand | 1718-1721 | 4 | 5 |
| β-strand | 1728-1729 | 2 | 5 |
| α-helix | 1731-1734 | 4 | |
| β-strand | 1743-1746 | 4 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1088-1103 | 16 | |
| α-helix | 1110-1112 | 3 | |
| α-helix | 1118-1121 | 4 | |
| α-helix | 1126-1129 | 4 | |
| α-helix | 1136-1145 | 10 | |
| α-helix | 1151-1168 | 18 | |
| α-helix | 1174-1196 | 23 | |
| β-strand | 1206 | 1 | 6 |
| α-helix | 1277 | 1 | |
| β-strand | 1278 | 1 | 6 |
| α-helix | 1279-1280 | 2 | |
| β-strand | 1281-1283 | 3 | 7 |
| β-strand | 1290-1292 | 3 | 7 |
| α-helix | 1293-1296 | 4 | |
| α-helix | 1310-1314 | 5 | |
| α-helix | 1320-1322 | 3 | |
| α-helix | 1331-1332 | 2 | |
| α-helix | 1334-1350 | 17 | |
| β-strand | 1358-1371 | 14 | 8 |
| α-helix | 1372-1373 | 2 | |
| α-helix | 1374-1376 | 3 | |
| α-helix | 1377-1381 | 5 | |
| β-strand | 1389-1403 | 15 | 8 |
| β-strand | 1406-1418 | 13 | 8 |
| α-helix | 1423 | 1 | |
| β-strand | 1429-1437 | 9 | 8 |
| α-helix | 1444-1446 | 3 | |
| α-helix | 1447-1465 | 19 | |
| β-strand | 1469-1473 | 5 | 8 |
| α-helix | 1497-1513 | 17 | |
| β-strand | 1519-1522 | 4 | 8 |
| α-helix | 1523-1529 | 7 | |
| α-helix | 1535-1537 | 3 | |
| α-helix | 1545-1555 | 11 | |
| α-helix | 1622-1628 | 7 | |
| α-helix | 1630-1632 | 3 | |
| β-strand | 1633-1637 | 5 | 8 |
| α-helix | 1648-1650 | 3 | |
| α-helix | 1655-1656 | 2 | |
| α-helix | 1660-1662 | 3 | |
| α-helix | 1666-1675 | 10 | |
| α-helix | 1682-1699 | 18 | |
| β-strand | 1707 | 1 | 9 |
| β-strand | 1714 | 1 | 9 |
| β-strand | 1718-1721 | 4 | 10 |
| β-strand | 1728-1729 | 2 | 10 |
| α-helix | 1731-1736 | 6 | |
| β-strand | 1743-1746 | 4 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| CREB-binding protein | A, B | protein | 621 | Mus musculus | P45481 (AlphaFold model) |
>5U7G_1 CREB-binding protein (chains A, B) GAMGSSQPRKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKNP MDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQEIDPV MQSLGYCCGRKYEFSPQTLCCYGKQLCTIPRDAAYYSYQNRYHFCEKCFTEIQGENVTLG DDPSQPQTTISKDQFEKKKNDTLDPEPFVDCKECGRKMHQICVLHYDIIWPSGFVCDNCL KKTGRPRKENKFSAKRLQTTRLGNHLEDRVNKFLRRQNHPEAGEVFVRVVASSDKTVEVK PGMKSRFVDSGEMSESFPYRTKALFAFEEIDGVDVCFFGMHVQEYGSDCPPPNTRRVYIS YLDSIHFFRPRCLRTAVYHEILIGYLEYVKKLGYVTGHIWACPPSEGDDYIFHCHPPDQK IPKPKRLQEWYKKMLDKAFAERIINDYKDIFKQANEDRLTSAKELPYFEGDFWPNVLEES IKESGGSGSQKLYATMEKHKEVFFVIHLHAGPVISTQPPIVDPDPLLSCDLMDGRDAFLT LARDKHWEFSSLRRSKWSTLCMLVELHTQGQDRFVYTCNECKHHVETRWHCTVCEDYDLC INCYNTKSHTHKMVKWGLGLD
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 8 |
Role of the CBP catalytic core in intramolecular SUMOylation and control of histone H3 acetylation. Park, S., Stanfield, R.L., Martinez-Yamout, M.A. et al. Proc Natl Acad Sci U S A (2017) 114:E5335-E5342. DOI 10.1073/pnas.1703105114 · PubMed
Other PDB entries of the same protein (UniProt P45481 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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