9SAF

Ternary PROTAC-mediated complex of BRD4-BD1/CRBN/DDB1 and JQ1-AcQ bifunctional degrader

This is a non-PDB format compatible entry.

Entity

Entity ID	Chain ID	Description	Type	Chain length	Formula weight	Number of molecules	DB Name (Accession)	Biological source	Descriptive keywords
1	A (A)	DNA damage-binding protein 1	polymer	836	93347.1	1	UniProt (Q16531) Pfam (PF10433) Pfam (PF03178)	Homo sapiens (human)	DDB p127 subunit,DNA damage-binding protein a,DDBa,Damage-specific DNA-binding protein 1,HBV X-associated protein 1,XAP-1,UV-damaged DNA-binding factor,UV-damaged DNA-binding protein 1,UV-DDB 1,XPE-binding factor,XPE-BF,Xeroderma pigmentosum group E-complementing protein,XPCe
2	B (B)	Protein cereblon	polymer	442	50559.6	1	UniProt (Q96SW2) Pfam (PF02190) Pfam (PF03226)	Homo sapiens (human)
3	C (C)	Bromodomain-containing protein 4	polymer	127	15099.4	1	UniProt (O60885) Pfam (PF00439)	Homo sapiens (human)	Protein HUNK1
4	D (B)	ZINC ION	non-polymer		65.4	1	Chemie (ZN)
5	E (B)	~{N}-[(2~{S})-1-[[(3~{S})-2,6-bis(oxidanylidene)piperidin-3-yl]amino]-1-oxidanylidene-propan-2-yl]-9-[2-[(9~{S})-7-(4-chlorophenyl)-4,5,13-trimethyl-3-thia-1,8,11,12-tetrazatricyclo[8.3.0.0^{2,6}]trideca-2(6),4,10,12-tetraen-9-yl]ethanoylamino]nonanamide	non-polymer		739.3	1	Chemie (A1JM8)
6	F, G (A, B)	water	water		18.0	89	Chemie (HOH)

Sequence modifications

A: 1 - 1138 (UniProt: Q16531)

PDB	External Database	Details
-	Ile 396	deletion
-	His 397	deletion
-	Glu 398	deletion
-	His 399	deletion
-	Ala 400	deletion
-	Ser 401	deletion
-	Ile 402	deletion
-	Asp 403	deletion
-	Leu 404	deletion
-	Pro 405	deletion
-	Gly 406	deletion
-	Ile 407	deletion
-	Lys 408	deletion
-	Gly 409	deletion
-	Leu 410	deletion
-	Trp 411	deletion
-	Pro 412	deletion
-	Leu 413	deletion
-	Arg 414	deletion
-	Ser 415	deletion
-	Asp 416	deletion
-	Pro 417	deletion
-	Asn 418	deletion
-	Arg 419	deletion
-	Glu 420	deletion
-	Thr 421	deletion
-	Asp 422	deletion
-	Asp 423	deletion
-	Thr 424	deletion
-	Leu 425	deletion
-	Val 426	deletion
-	Leu 427	deletion
-	Ser 428	deletion
-	Phe 429	deletion
-	Val 430	deletion
-	Gly 431	deletion
-	Gln 432	deletion
-	Thr 433	deletion
-	Arg 434	deletion
-	Val 435	deletion
-	Leu 436	deletion
-	Met 437	deletion
-	Leu 438	deletion
-	Asn 439	deletion
-	Gly 440	deletion
-	Glu 441	deletion
-	Glu 442	deletion
-	Val 443	deletion
-	Glu 444	deletion
-	Glu 445	deletion
-	Thr 446	deletion
-	Glu 447	deletion
-	Leu 448	deletion
-	Met 449	deletion
-	Gly 450	deletion
-	Phe 451	deletion
-	Val 452	deletion
-	Asp 453	deletion
-	Asp 454	deletion
-	Gln 455	deletion
-	Gln 456	deletion
-	Thr 457	deletion
-	Phe 458	deletion
-	Phe 459	deletion
-	Cys 460	deletion
-	Val 463	deletion
-	Ala 464	deletion
-	His 465	deletion
-	Gln 466	deletion
-	Gln 467	deletion
-	Leu 468	deletion
-	Ile 469	deletion
-	Gln 470	deletion
-	Ile 471	deletion
-	Thr 472	deletion
-	Ser 473	deletion
-	Ala 474	deletion
-	Ser 475	deletion
-	Val 476	deletion
-	Arg 477	deletion
-	Leu 478	deletion
-	Val 479	deletion
-	Ser 480	deletion
-	Gln 481	deletion
-	Glu 482	deletion
-	Pro 483	deletion
-	Lys 484	deletion
-	Ala 485	deletion
-	Leu 486	deletion
-	Val 487	deletion
-	Ser 488	deletion
-	Glu 489	deletion
-	Trp 490	deletion
-	Lys 491	deletion
-	Glu 492	deletion
-	Pro 493	deletion
-	Gln 494	deletion
-	Ala 495	deletion
-	Lys 496	deletion
-	Asn 497	deletion
-	Ile 498	deletion
-	Ser 499	deletion
-	Val 500	deletion
-	Ala 501	deletion
-	Ser 502	deletion
-	Cys 503	deletion
-	Asn 504	deletion
-	Ser 505	deletion
-	Ser 506	deletion
-	Gln 507	deletion
-	Val 508	deletion
-	Val 509	deletion
-	Val 510	deletion
-	Ala 511	deletion
-	Val 512	deletion
-	Gly 513	deletion
-	Arg 514	deletion
-	Ala 515	deletion
-	Leu 516	deletion
-	Tyr 517	deletion
-	Tyr 518	deletion
-	Leu 519	deletion
-	Gln 520	deletion
-	Ile 521	deletion
-	His 522	deletion
-	Pro 523	deletion
-	Gln 524	deletion
-	Glu 525	deletion
-	Leu 526	deletion
-	Arg 527	deletion
-	Gln 528	deletion
-	Ile 529	deletion
-	Ser 530	deletion
-	His 531	deletion
-	Thr 532	deletion
-	Glu 533	deletion
-	Met 534	deletion
-	Glu 535	deletion
-	His 536	deletion
-	Glu 537	deletion
-	Val 538	deletion
-	Ala 539	deletion
-	Cys 540	deletion
-	Leu 541	deletion
-	Asp 542	deletion
-	Ile 543	deletion
-	Thr 544	deletion
-	Pro 545	deletion
-	Leu 546	deletion
-	Gly 547	deletion
-	Asp 548	deletion
-	Ser 549	deletion
-	Asn 550	deletion
-	Gly 551	deletion
-	Leu 552	deletion
-	Ser 553	deletion
-	Pro 554	deletion
-	Leu 555	deletion
-	Cys 556	deletion
-	Ala 557	deletion
-	Ile 558	deletion
-	Gly 559	deletion
-	Leu 560	deletion
-	Trp 561	deletion
-	Thr 562	deletion
-	Asp 563	deletion
-	Ile 564	deletion
-	Ser 565	deletion
-	Ala 566	deletion
-	Arg 567	deletion
-	Ile 568	deletion
-	Leu 569	deletion
-	Lys 570	deletion
-	Leu 571	deletion
-	Pro 572	deletion
-	Ser 573	deletion
-	Phe 574	deletion
-	Glu 575	deletion
-	Leu 576	deletion
-	Leu 577	deletion
-	His 578	deletion
-	Lys 579	deletion
-	Glu 580	deletion
-	Met 581	deletion
-	Leu 582	deletion
-	Gly 583	deletion
-	Gly 584	deletion
-	Glu 585	deletion
-	Ile 586	deletion
-	Ile 587	deletion
-	Pro 588	deletion
-	Arg 589	deletion
-	Ser 590	deletion
-	Ile 591	deletion
-	Leu 592	deletion
-	Met 593	deletion
-	Thr 594	deletion
-	Thr 595	deletion
-	Phe 596	deletion
-	Glu 597	deletion
-	Ser 598	deletion
-	Ser 599	deletion
-	His 600	deletion
-	Tyr 601	deletion
-	Leu 602	deletion
-	Leu 603	deletion
-	Cys 604	deletion
-	Ala 605	deletion
-	Leu 606	deletion
-	Gly 607	deletion
-	Asp 608	deletion
-	Gly 609	deletion
-	Ala 610	deletion
-	Leu 611	deletion
-	Phe 612	deletion
-	Tyr 613	deletion
-	Phe 614	deletion
-	Gly 615	deletion
-	Leu 616	deletion
-	Asn 617	deletion
-	Ile 618	deletion
-	Glu 619	deletion
-	Thr 620	deletion
-	Gly 621	deletion
-	Leu 622	deletion
-	Leu 623	deletion
-	Ser 624	deletion
-	Asp 625	deletion
-	Arg 626	deletion
-	Lys 627	deletion
-	Lys 628	deletion
-	Val 629	deletion
-	Thr 630	deletion
-	Leu 631	deletion
-	Gly 632	deletion
-	Thr 633	deletion
-	Gln 634	deletion
-	Pro 635	deletion
-	Thr 636	deletion
-	Val 637	deletion
-	Leu 638	deletion
-	Arg 639	deletion
-	Thr 640	deletion
-	Phe 641	deletion
-	Arg 642	deletion
-	Ser 643	deletion
-	Leu 644	deletion
-	Ser 645	deletion
-	Thr 646	deletion
-	Thr 647	deletion
-	Asn 648	deletion
-	Val 649	deletion
-	Phe 650	deletion
-	Ala 651	deletion
-	Cys 652	deletion
-	Ser 653	deletion
-	Asp 654	deletion
-	Arg 655	deletion
-	Pro 656	deletion
-	Thr 657	deletion
-	Val 658	deletion
-	Ile 659	deletion
-	Tyr 660	deletion
-	Ser 661	deletion
-	Ser 662	deletion
-	Asn 663	deletion
-	His 664	deletion
-	Lys 665	deletion
-	Leu 666	deletion
-	Val 667	deletion
-	Phe 668	deletion
-	Ser 669	deletion
-	Asn 670	deletion
-	Val 671	deletion
-	Asn 672	deletion
-	Leu 673	deletion
-	Lys 674	deletion
-	Glu 675	deletion
-	Val 676	deletion
-	Asn 677	deletion
-	Tyr 678	deletion
-	Met 679	deletion
-	Cys 680	deletion
-	Pro 681	deletion
-	Leu 682	deletion
-	Asn 683	deletion
-	Ser 684	deletion
-	Asp 685	deletion
-	Tyr 687	deletion
-	Pro 688	deletion
-	Asp 689	deletion
-	Ser 690	deletion
-	Leu 691	deletion
-	Ala 692	deletion
-	Leu 693	deletion
-	Ala 694	deletion
-	Asn 695	deletion
-	Thr 698	deletion
-	Leu 699	deletion
-	Thr 700	deletion
-	Ile 701	deletion
-	Thr 703	deletion
-	Ile 704	deletion
-	Asp 705	deletion

B: 2 - 442 (UniProt: Q96SW2)

PDB	External Database	Details
Ser 1	-	expression tag

C: 44 - 168 (UniProt: O60885)

PDB	External Database	Details
Ser 42	-	expression tag
Met 43	-	expression tag

Contents of the asymmetric unit

Polymers	Number of chains	3
	Total formula weight	159006.0
Non-Polymers*	Number of molecules	2
	Total formula weight	804.7
All*	Total formula weight	159810.8

*Water molecules are not included.