1F3U: RAP30/74 interaction domains of human tfiif

Crystal structure of the RAP30/74 interaction domains of human tfiif. Determined by X-ray diffraction at 1.7 Å resolution. Released 11 Oct 2000.

Method: X-ray diffraction
Resolution: 1.7 Å
Organism: Homo sapiens
Chains: 8
Atoms: 9,192
Mol. weight: 130.64 kDa
Released: 11 Oct 2000

Explore 1F3U in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1F3U contains 47 α-helices and 66 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: 5 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	6-8	3	1
α-helix	10-13	4
β-strand	17-24	8	1
α-helix	25-31	7
β-strand	39-48	10	1
β-strand	51-58	8	1
α-helix	60-63	4
α-helix	78-79	2
β-strand	80-86	7	1
β-strand	92-99	8	1
β-strand	104-116	13	1
α-helix	117-118	2

Chain B: 6 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	10-17	8	1
β-strand	24-31	8	1
α-helix	33-35	3
α-helix	39-41	3
β-strand	45-49	5	1
α-helix	52-55	4
β-strand	58-61	4	2
α-helix	76-78	3
β-strand	84-87	4	2
α-helix	97	1
β-strand	98-102	5	1
β-strand	109-114	6	1
β-strand	122-129	8	1
β-strand	135-148	14	1
α-helix	149-151	3

Chain C: 3 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	6	1	3
β-strand	8	1	3
α-helix	10-13	4
β-strand	17-24	8	3
α-helix	25-31	7
β-strand	39-48	10	3
β-strand	51-58	8	3
α-helix	60-63	4
β-strand	80-86	7	3
β-strand	91-99	9	3
β-strand	104-116	13	3

Chain D: 10 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	10-17	8	3
β-strand	24-32	9	3
α-helix	33-35	3
α-helix	39-41	3
β-strand	45-49	5	3
β-strand	57-61	5	4
α-helix	75-78	4
α-helix	79-81	3
β-strand	84-88	5	4
α-helix	90-92	3
α-helix	93-95	3
α-helix	97	1
β-strand	98-102	5	3
β-strand	109-114	6	3
α-helix	115-116	2
β-strand	122-129	8	3
β-strand	135-148	14	3
α-helix	149-151	3
α-helix	157-167	11

Chain E: 4 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	6-8	3	5
α-helix	10-13	4
β-strand	17-24	8	5
α-helix	25-31	7
β-strand	39-48	10	5
β-strand	51-58	8	5
α-helix	60-63	4
α-helix	77-79	3
β-strand	80-86	7	5
β-strand	91-99	9	5
β-strand	104-116	13	5

Chain F: 7 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	11-17	7	5
β-strand	24-32	9	5
α-helix	33-35	3
α-helix	39-41	3
β-strand	45-49	5	5
β-strand	55-61	7	6
β-strand	84-90	7	6
α-helix	93-95	3
α-helix	97	1
β-strand	98-102	5	5
β-strand	109-114	6	5
α-helix	115-116	2
β-strand	122-129	8	5
β-strand	135-148	14	5
α-helix	149-151	3
α-helix	157-167	11

Chain G: 5 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	6-8	3	7
α-helix	10-13	4
β-strand	17-24	8	7
α-helix	25-31	7
β-strand	35	1	7
β-strand	39-48	10	7
β-strand	51-58	8	7
α-helix	60-63	4
α-helix	77-80	4
β-strand	81-86	6	7
β-strand	91-98	8	7
β-strand	104-116	13	7
α-helix	117-118	2

Chain H: 7 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	12-17	6	7
β-strand	25-32	8	7
α-helix	33-35	3
α-helix	39-41	3
β-strand	45-49	5	7
α-helix	52-54	3
β-strand	58-61	4	8
α-helix	76-78	3
α-helix	82-83	2
β-strand	84-87	4	8
α-helix	97	1
β-strand	98-102	5	7
β-strand	109-114	6	7
β-strand	122-129	8	7
β-strand	135-148	14	7
α-helix	149-151	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Transcription initiation factor iif, beta subunit	A, C, E, G	protein	118	Homo sapiens	P13984 (AlphaFold model)
Transcription initiation factor iif, alpha subunit	B, D, F, H	protein	171	Homo sapiens	P35269 (AlphaFold model)

Sequence of entity 1 (A, C, E, G), FASTA

>1F3U_1 TRANSCRIPTION INITIATION FACTOR IIF, BETA SUBUNIT (chains A, C, E, G)
AERGELDLTGAKQNTGVWLVKVPKYLSQQWAKASGRGEVGKLRIAKTQGRTEVSFTLNED
LANIHDIGGKPASVSAPREHPFVLQSVGGQTLTVFTESSSDKLSLEGIVVQRAECRPA

Sequence of entity 2 (B, D, F, H), FASTA

>1F3U_2 TRANSCRIPTION INITIATION FACTOR IIF, ALPHA SUBUNIT (chains B, D, F, H)
AALGPSSQNVTEYVVRVPKNTTKKYNIMAFNAADKVNFATWNQARLERDLSNKKIYQEEE
MPESGAGSEFNRKLREEARRKKYGIVLKEFRPEDQPWLLRVNGKSGRKFKGIKKGGVTEN
TSYYIFTQCPDGAFEAFPVHNWYNFTPLARHRTLTAEEAEEEWERRNKVLN

Primary citation

Novel dimerization fold of RAP30/RAP74 in human TFIIF at 1.7 A resolution. Gaiser, F., Tan, S., Richmond, T.J. J Mol Biol (2000) 302:1119-1127. DOI 10.1006/jmbi.2000.4110 · PubMed

Other PDB entries of the same protein (UniProt P13984 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7NVU 2.5 Å, RNA polymerase II core pre-initiation complex with open promoter DNA
8WAV 2.72 Å, De novo transcribing complex 12 (TC12), the early elongation complex with Pol II…
8WAX 2.75 Å, De novo transcribing complex 14 (TC14), the early elongation complex with Pol II…
8WAZ 2.76 Å, De novo transcribing complex 16 (TC16), the early elongation complex with Pol II…
8WAU 2.78 Å, De novo transcribing complex 11 (TC11), the early elongation complex with Pol II…
7NVS 2.8 Å, RNA polymerase II core pre-initiation complex with closed promoter DNA in proximal…
8WAT 2.82 Å, De novo transcribing complex 10 (TC10), the early elongation complex with Pol II…
8WAY 2.85 Å, De novo transcribing complex 15 (TC15), the early elongation complex with Pol II…
7NVT 2.9 Å, RNA polymerase II core pre-initiation complex with closed promoter DNA in distal position
8S52 2.9 Å, RNA polymerase II core initially transcribing complex with an ordered RNA of 10 nt
8WB0 2.94 Å, De novo transcribing complex 17 (TC17), the early elongation complex with Pol II…
7ZWD 3.0 Å, Structure of SNAPc containing Pol II pre-initiation complex bound to U5 snRNA promoter…

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