2PK2: Cyclin-T1, Protein Tat

Cyclin box structure of the P-TEFb subunit Cyclin T1 derived from a fusion complex with EIAV Tat. Determined by X-ray diffraction at 2.67 Å resolution. Released 3 Jul 2007.

Method: X-ray diffraction
Resolution: 2.67 Å
Organisms: Homo sapiens, Equine infectious anemia virus
Chains: 4
Atoms: 8,396
Mol. weight: 161.37 kDa
Released: 3 Jul 2007

Explore 2PK2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2PK2 contains 74 α-helices and 0 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.

Chain A: 19 helices, 0 β-strands

Element	Residues	Length
α-helix	17-20	4
α-helix	25-28	4
α-helix	31-49	19
α-helix	56-69	14
α-helix	80-94	15
α-helix	101-105	5
α-helix	108-112	5
α-helix	117-119	3
α-helix	124-127	4
α-helix	128-130	3
α-helix	132-134	3
α-helix	136-143	8
α-helix	155-163	9
α-helix	168-181	14
α-helix	187-189	3
α-helix	193-196	4
α-helix	204-207	4
α-helix	231-244	14
α-helix	251-257	7

Chain B: 18 helices, 0 β-strands

Element	Residues	Length
α-helix	10-12	3
α-helix	23-28	6
α-helix	31-46	16
α-helix	56-69	14
α-helix	80-94	15
α-helix	101-105	5
α-helix	108-112	5
α-helix	117-119	3
α-helix	124-132	9
α-helix	136-143	8
α-helix	155-162	8
α-helix	168-183	16
α-helix	187-189	3
α-helix	193-196	4
α-helix	204-207	4
α-helix	221-223	3
α-helix	231-246	16
α-helix	251-258	8

Chain C: 18 helices, 0 β-strands

Element	Residues	Length
α-helix	16-18	3
α-helix	23-25	3
α-helix	31-33	3
α-helix	37-44	8
α-helix	45-49	5
α-helix	56-61	6
α-helix	64-72	9
α-helix	84-94	11
α-helix	103-112	10
α-helix	129-133	5
α-helix	134-141	8
α-helix	157-164	8
α-helix	175-183	9
α-helix	195-205	11
α-helix	221-223	3
α-helix	231-247	17
α-helix	252-257	6
α-helix	258-260	3

Chain D: 19 helices, 0 β-strands

Element	Residues	Length
α-helix	17-20	4
α-helix	23-27	5
α-helix	31-49	19
α-helix	56-69	14
α-helix	80-94	15
α-helix	101-105	5
α-helix	108-112	5
α-helix	117-119	3
α-helix	124-132	9
α-helix	136-143	8
α-helix	155-163	9
α-helix	168-183	16
α-helix	193-196	4
α-helix	204	1
α-helix	205-209	5
α-helix	221-223	3
α-helix	232-246	15
α-helix	251-256	6
α-helix	257-259	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cyclin-T1, Protein Tat	A, B, C, D	protein	358	Homo sapiens, Equine infectious anemia virus	O60563 (AlphaFold model), P32544

Sequence of entity 1 (A, B, C, D), FASTA

>2PK2_1 Cyclin-T1, Protein Tat (chains A, B, C, D)
MEGERKNNNKRWYFTREQLENSPSRRFGVDPDKELSYRQQAANLLQDMGQRLNVSQLTIN
TAIVYMHRFYMIQSFTRFPGNSVAPAALFLAAKVEEQPKKLEHVIKVAHTCLHPQESLPD
TRSEAYLQQVQDLVILESIILQTLGFELTIDHPHTHVVKCTQLVRASKDLAQTSYFMATN
SLHLTTFSLQYTPPVVACVCIHLACKWSNWEIPVSTDGKHWWEYVDATVTLELLDELTHE
FLQILEKTPNRLKRIWNWRACEAAKKTKADDRGTDEKTSEQGGTGGGSGGGSGGGSGGGT
SGGVPGQNTGGQEARPNYHCQLCFLRSLGIDYLDASLRKKNKQRLKAIQQGRQPQYLL

Primary citation

Cyclin Box Structure of the P-TEFb Subunit Cyclin T1 Derived from a Fusion Complex with EIAV Tat. Anand, K., Schulte, A., Fujinaga, K. et al. J Mol Biol (2007) 370:826-836. DOI 10.1016/j.jmb.2007.04.077 · PubMed

Other PDB entries of the same protein (UniProt O60563 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3MI9 2.1 Å, Crystal structure of HIV-1 Tat complexed with human P-TEFb
3BLH 2.48 Å, Crystal Structure of Human CDK9/cyclinT1
3BLR 2.8 Å, Crystal Structure of Human CDK9/cyclinT1 in complex with Flavopiridol
3MY1 2.8 Å, Structure of CDK9/cyclinT1 in complex with DRB
7NWK 2.81 Å, Crystal structure of CDK9-Cyclin T1 bound by compound 6
3BLQ 2.9 Å, Crystal Structure of Human CDK9/cyclinT1 in Complex with ATP
4OR5 2.9 Å, Crystal structure of HIV-1 Tat complexed with human P-TEFb and AFF4
4IMY 2.94 Å, The AFF4 scaffold binds human P-TEFb adjacent to HIV Tat
3TN8 2.95 Å, CDK9/cyclin T in complex with CAN508
4BCH 2.96 Å, Structure of CDK9 in complex with cyclin T and a 2-amino-4-heteroaryl- pyrimidine…
3LQ5 3.0 Å, Structure of CDK9/CyclinT in complex with S-CR8
3MIA 3.0 Å, Crystal structure of HIV-1 Tat complexed with ATP-bound human P-TEFb

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