3VD1: Tumor protein p73

structure of p73 DNA binding domain tetramer modulates p73 transactivation. Determined by X-ray diffraction at 2.95 Å resolution. Released 18 Apr 2012.

Method: X-ray diffraction
Resolution: 2.95 Å
Organism: Homo sapiens
Chains: 16
Atoms: 14,716
Mol. weight: 220.05 kDa
Ligands: ZN
Released: 18 Apr 2012

Explore 3VD1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3VD1 contains 35 α-helices and 107 β-strands across 8 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.

Chain A: 4 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	121	1	1
β-strand	128-130	3	2
β-strand	142-143	2	1
β-strand	150-153	4	1
β-strand	159-164	6	2
α-helix	168-170	3
β-strand	174-181	8	1
α-helix	184-187	4
α-helix	195-199	5
β-strand	215-217	3	2
β-strand	224-228	5	1
β-strand	233-239	7	1
β-strand	250-256	7	2
β-strand	261	1	3
β-strand	267	1	3
β-strand	271-278	8	1
β-strand	286-288	3	1
β-strand	291-294	4	1
α-helix	298-309	12

Chain B: 5 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	121	1	4
β-strand	127-131	5	5
α-helix	134-136	3
β-strand	142-145	4	4
β-strand	150-153	4	4
β-strand	159-165	7	5
β-strand	174-181	8	4
α-helix	184-187	4
α-helix	195-199	5
β-strand	215-217	3	5
β-strand	224-227	4	4
β-strand	234-239	6	4
α-helix	242-244	3
β-strand	249-256	8	5
β-strand	271-278	8	4
β-strand	284-294	11	4
α-helix	298-311	14

Chain C: 3 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	121	1	6
β-strand	128-130	3	7
β-strand	142-145	4	6
β-strand	150-154	5	6
β-strand	159-164	6	7
α-helix	168-170	3
β-strand	174-181	8	6
α-helix	195-198	4
β-strand	215-217	3	7
β-strand	224-227	4	6
β-strand	234-239	6	6
β-strand	250-256	7	7
β-strand	271-278	8	6
β-strand	284-295	12	6
α-helix	298-311	14

Chain D: 4 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	121	1	8
β-strand	128-130	3	9
β-strand	142-145	4	10
β-strand	150-153	4	10
β-strand	159-164	6	9
β-strand	173-181	9	10
α-helix	186-188	3
β-strand	190	1	10
α-helix	195-198	4
β-strand	215-217	3	9
β-strand	224-227	4	10
β-strand	234-239	6	10
α-helix	242-244	3
β-strand	250-256	7	9
β-strand	271-279	9	10
β-strand	284	1	10
β-strand	287	1	8
β-strand	288-294	7	10
α-helix	298-311	14

Chain I: 4 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	121	1	11
β-strand	128-131	4	12
β-strand	142-145	4	11
β-strand	150-153	4	11
β-strand	158-164	7	12
α-helix	169-170	2
β-strand	174-181	8	11
α-helix	195-198	4
β-strand	215-217	3	12
β-strand	224-227	4	11
β-strand	234-239	6	11
α-helix	242-244	3
β-strand	250-256	7	12
β-strand	271-278	8	11
β-strand	284-294	11	11
α-helix	298-310	13

Chain J: 5 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	123-125	3
β-strand	128-131	4	13
β-strand	142-145	4	14
β-strand	150-153	4	14
β-strand	159-164	6	13
β-strand	174-181	8	14
α-helix	184-187	4
α-helix	190-191	2
α-helix	195-199	5
β-strand	215-217	3	13
β-strand	224	1	14
β-strand	227	1	15
β-strand	234	1	15
β-strand	236-238	3	14
β-strand	245	1	16
β-strand	247	1	16
β-strand	252-256	5	13
β-strand	271-278	8	14
β-strand	284-292	9	14
α-helix	298-311	14

Chain K: 4 helices, 13 β-strands

Element	Residues	Length	Sheet
α-helix	116-117	2
β-strand	121	1	17
β-strand	130	1	18
β-strand	142-145	4	19
β-strand	150-154	5	19
β-strand	159-163	5	18
α-helix	167-168	2
β-strand	174-181	8	19
α-helix	195-198	4
β-strand	215-217	3	18
β-strand	225-227	3	19
β-strand	234-239	6	19
β-strand	250-256	7	18
β-strand	271-278	8	19
β-strand	287	1	17
β-strand	288-295	8	19
α-helix	298-310	13

Chain L: 6 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	121	1	20
β-strand	128-130	3	21
β-strand	142-144	3	20
β-strand	151-154	4	20
β-strand	155	1	21
β-strand	159-164	6	21
α-helix	168-170	3
β-strand	174-181	8	20
α-helix	184-186	3
α-helix	190-191	2
α-helix	195-199	5
β-strand	215-217	3	21
β-strand	224-227	4	20
β-strand	234-239	6	20
α-helix	242-244	3
β-strand	250-256	7	21
β-strand	271-278	8	20
β-strand	284-295	12	20
α-helix	300-310	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Tumor protein p73	A, B, C, D, I, J, K, L	protein	210	Homo sapiens	O15350 (AlphaFold model)
DNA (5'-d(cpgpgpgpcpaptpgpcpcpcpg)-3')	E, F, G, H, M, N, O, P	DNA	12

Sequence of entity 1 (A, B, C, D, I, J, K, L), FASTA

>3VD1_1 Tumor protein p73 (chains A, B, C, D, I, J, K, L)
MGHHHHHHHHEFIPSNTDYPGPHHFEVTFQQSSTAKSATWTYSPLLKKLYCQIAKTCPIQ
IKVSTPPPPGTAIRAMPVYKKAEHVTDVVKRCPNHELGRDFNEGQSAPASHLIRVEGNNL
SQYVDDPVTGRQSVVVPYEPPQVGTEFTTILYNFMCNSSCVGGMNRRPILIIITLEMRDG
QVLGRRSFEGRICACPGRDRKADEDHYREQ

Sequence of entity 2 (E, F, G, H, M, N, O, P), FASTA

>3VD1_2 DNA (5'-D(*CP*GP*GP*GP*CP*AP*TP*GP*CP*CP*CP*G)-3') (chains E, F, G, H, M, N, O, P)
CGGGCATGCCCG

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	8

Primary citation

Structure of p73 DNA-binding domain tetramer modulates p73 transactivation. Ethayathulla, A.S., Tse, P.W., Monti, P. et al. Proc Natl Acad Sci U S A (2012) 109:6066-6071. DOI 10.1073/pnas.1115463109 · PubMed

Other PDB entries of the same protein (UniProt O15350 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5HOB 1.22 Å, p73 homo-tetramerization domain mutant I
5HOC 1.36 Å, p73 homo-tetramerization domain mutant II
2WQI 1.7 Å, Crystal structure of the human p73 tetramerization domain
8P9C 1.76 Å, Crystal structure of p63-p73 heterotetramer (tetramerisation domain) in complex with…
9GNB 1.8 Å, Structure of p73 SAM domain in complex with DARPin B9
2XWC 1.82 Å, Crystal structure of the DNA binding domain of human TP73 refined at 1.8 A resolution
2WQJ 2.0 Å, Crystal structure of a truncated variant of the human p73 tetramerization domain
9GLQ 2.1 Å, Crystal structure of p73 tetramerisation domain in complex with darpins 1800
8P9E 2.25 Å, Crystal structure of wild type p63-p73 heterotetramer (tetramerisation domain) in…
4A63 2.27 Å, Crystal structure of the p73-ASPP2 complex at 2.6A resolution
2WTT 2.3 Å, Structure of the human p73 tetramerization domain (crystal form II)
1DXS 2.54 Å, Crystal structure of the C-terminal sterile alpha motif (SAM) domain of human p73 alpha…

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