5O85: P34-p44 complex

Name: PDB 5O85: p34-p44 complex
Published: 2017-10-18
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: transcription

p34-p44 complex. Determined by X-ray diffraction at 3.4 Å resolution. Released 18 Oct 2017.

Method: X-ray diffraction
Resolution: 3.4 Å
Organism: Homo sapiens
Chains: 4
Atoms: 3,849
Mol. weight: 158.03 kDa
Ligands: ZN
Released: 18 Oct 2017

Explore 5O85 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5O85 contains 25 α-helices and 17 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: 10 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	10-15	6	1
α-helix	19-27	9
α-helix	34-51	18
β-strand	56-62	7	1
β-strand	67-71	5	1
α-helix	106-120	15
β-strand	131	1	2
α-helix	133-150	18
β-strand	160-165	6	1
α-helix	168	1
β-strand	169	1	2
α-helix	170	1
α-helix	174-186	13
β-strand	190-195	6	1
α-helix	201-210	10
β-strand	214-216	3	1
α-helix	220-222	3
α-helix	223-230	8

Chain B: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	369-374	6
α-helix	375-379	5
α-helix	383-386	4

Chain C: 8 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	9-16	8	3
α-helix	19-27	9
α-helix	34-51	18
β-strand	56-62	7	3
β-strand	67-71	5	3
α-helix	103-121	19
α-helix	133-150	18
β-strand	158-165	8	3
α-helix	174-186	13
β-strand	190-195	6	3
α-helix	201-210	10
β-strand	214-216	3	3
α-helix	220-222	3
α-helix	223-230	8

Chain D: 4 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	329-331	3
β-strand	332-333	2	4
β-strand	358-359	2	4
β-strand	366-367	2	4
α-helix	369-374	6
α-helix	375-379	5
α-helix	383-386	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
General transcription factor IIH subunit 3	A, C	protein	308	Homo sapiens	Q13889 (AlphaFold model)
General transcription factor IIH subunit 2	B, D	protein	395	Homo sapiens	Q13888 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>5O85_1 General transcription factor IIH subunit 3 (chains A, C)
MVSDEDELNLLVIVVDANPIWWGKQALKESQFTLSKCIDAVMVLGNSHLFMNRSNKLAVI
ASHIQESRFLYPGKNGRLGDFFGDPGNPPEFNPSGSKDGKYELLTSANEVIVEEIKDLMT
KSDIKGQHTETLLAGSLAKALCYIHRMNKEVKDNQEMKSRILVIKAAEDSALQYMNFMNV
IFAAQKQNILIDACVLDSDSGLLQQACDITGGLYLKVPQMPSLLQYLLWVFLPDQDQRSQ
LILPPPVHVDYRAACFCHRNLIEIGYVCSVCLSIFCNFSPICTTCETAFKISLPPVLKAK
KKKLKVSA

Sequence of entity 2 (B, D), FASTA

>5O85_2 General transcription factor IIH subunit 2 (chains B, D)
MDEEPERTKRWEGGYERTWEILKEDESGSLKATIEDILFKAKRKRVFEHHGQVRLGMMRH
LYVVVDGSRTMEDQDLKPNRLTCTLKLLEYFVEEYFDQNPISQIGIIVTKSKRAEKLTEL
SGNPRKHITSLKKAVDMTCHGEPSLYNSLSIAMQTLKHMPGHTSREVLIIFSSLTTCDPS
NIYDLIKTLKAAKIRVSVIGLSAEVRVCTVLARETGGTYHVILDESHYKELLTHHVSPPP
ASSSSECSLIRMGFPQHTIASLSDQDAKPSFSMAHLDGNTEPGLTLGGYFCPQCRAKYCE
LPVECKICGLTLVSAPHLARSYHHLFPLDAFQEIPLEEYNGERFCYGCQGELKDQHVYVC
AVCQNVFCVDCDVFVHDSLHSCPGCIHKIPAPSGV

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	4

Primary citation

The intricate network between the p34 and p44 subunits is central to the activity of the transcription/DNA repair factor TFIIH. Radu, L., Schoenwetter, E., Braun, C. et al. Nucleic Acids Res (2017) 45:10872-10883. DOI 10.1093/nar/gkx743 · PubMed

Other PDB entries of the same protein (UniProt Q13889 (AlphaFold model), which also has an AlphaFold model), best resolution first:

28JM 3.29 Å, Cryo-EM structure of the human holo-TFIIH and XPC initial encounter complex
7EGB 3.3 Å, TFIID-based holo PIC on SCP promoter
8EBU 3.3 Å, XPC release from Core7-XPA-DNA (Cy5)
9PD3 3.3 Å, NER dual incision complex - DuIS
28JS 3.32 Å, Cryo-EM structure of the human holo-TFIIH-XPC complex bound to bulky lesion-mimic DNA…
9PD4 3.4 Å, NER dual incision complex - DuIM
6RO4 3.5 Å, Structure of the core TFIIH-XPA-DNA complex
7AD8 3.5 Å, Core TFIIH-XPA-DNA complex with modelled p62 subunit
9XYU 3.5 Å, NER complex - C7CAD.ATP
28KE 3.6 Å, Cryo-EM structure of the human holo-TFIIH-XPC-XPA complex bound to bulky lesion-mimic DNA
8EBX 3.6 Å, XPA repositioning Core7 of TFIIH relative to XPC-DNA lesion (AP)
8EBY 3.6 Å, XPC release from Core7-XPA-DNA (AP)

Browse structure collections

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