2FFH: Protein

The signal sequence binding protein ffh from thermus aquaticus. Determined by X-ray diffraction at 3.2 Å resolution. Released 16 Jul 1999.

Method: X-ray diffraction
Resolution: 3.2 Å
Organism: Thermus aquaticus
Chains: 3
Atoms: 9,484
Mol. weight: 142.52 kDa
Ligands: CD
Released: 16 Jul 1999

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

Secondary structure: helices and β-sheets

2FFH contains 72 α-helices and 24 β-strands across 3 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: 24 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	3-14	12
α-helix	24-40	17
α-helix	45-60	16
α-helix	64-66	3
α-helix	70-85	16
β-strand	99-104	6	1
α-helix	111-123	13
β-strand	129-133	5	1
α-helix	139-152	14
β-strand	156-158	3	1
α-helix	165-178	14
β-strand	183-187	5	1
α-helix	196-209	14
β-strand	213-219	7	1
α-helix	220-222	3
α-helix	225-236	12
β-strand	241-245	5	1
α-helix	247-249	3
α-helix	254-263	10
β-strand	267-271	5	1
α-helix	276-278	3
β-strand	279-281	3	1
α-helix	284-292	9
α-helix	300-306	7
α-helix	322-334	13
α-helix	341-343	3
α-helix	348	1
α-helix	356-367	12
α-helix	371-375	5
α-helix	377-379	3
α-helix	382-392	11
α-helix	396-415	20

Chain B: 24 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	3-15	13
α-helix	24-40	17
α-helix	45-60	16
α-helix	64-66	3
α-helix	71-85	15
β-strand	99-105	7	2
α-helix	111-123	13
β-strand	129-133	5	2
α-helix	139-152	14
β-strand	156-158	3	2
α-helix	165-179	15
β-strand	183-187	5	2
α-helix	196-209	14
β-strand	213-219	7	2
α-helix	220-222	3
α-helix	224-236	13
β-strand	241-245	5	2
α-helix	247-249	3
α-helix	254-263	10
β-strand	267-271	5	2
α-helix	276-278	3
β-strand	279-281	3	2
α-helix	284-292	9
α-helix	300-305	6
α-helix	322-334	13
α-helix	341-344	4
α-helix	347-348	2
α-helix	356-367	12
α-helix	371-375	5
α-helix	377-379	3
α-helix	382-392	11
α-helix	396-415	20

Chain C: 24 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	3-14	12
α-helix	24-39	16
α-helix	45-60	16
α-helix	64-66	3
α-helix	70-85	16
α-helix	93-95	3
β-strand	99-105	7	3
α-helix	111-123	13
β-strand	129-133	5	3
α-helix	139-152	14
β-strand	156-158	3	3
α-helix	165-179	15
β-strand	183-187	5	3
α-helix	196-209	14
β-strand	213-219	7	3
α-helix	220-222	3
α-helix	225-236	12
β-strand	241-245	5	3
α-helix	247-249	3
α-helix	254-263	10
β-strand	267-271	5	3
α-helix	276-278	3
β-strand	279-281	3	3
α-helix	284-291	8
α-helix	300-306	7
α-helix	322-334	13
α-helix	347-348	2
α-helix	356-368	13
α-helix	371-375	5
α-helix	377-379	3
α-helix	382-392	11
α-helix	396-415	20

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein (FFH)	A, B, C	protein	425	Thermus aquaticus	O07347 (AlphaFold model)

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

>2FFH_1 PROTEIN (FFH) (chains A, B, C)
MFQQLSARLQEAIGRLRGRGRITEEDLKATLREIRRALMDADVNLEVTRDFVERVREEAL
GKQVLESLTPAEVILATVYEALKEALGGEARLPVLKDRNLWFLVGLQGSGKTTTAAKLAL
YYKGKGRRPLLVAADTQRPAAREQLRLLGEKVGVPVLEVMDGESPESIRRRVEEKARLEA
RDLILVDTAGRLQIDEPLMGELARLKEVLGPDEVLLVLDAMTGQEALSVARAFDEKVGVT
GLVLTKLDGDARGGAALSARHVTGKPIYFAGVSEKPEGLEPFYPERLAGRILGMGDVASL
AEKVRAAGLEAEAPKSAKELSLEDFLKQMQNLKRLGPFSEILGLLPGVPQGLKVDEKAIK
RLEAIVLSMTPEERKDPRILNGSRRKRIAKGSGTSVQEVNRFIKAFEEMKALMKSLEKKK
GRGLM

Ligands and cofactors

ID	Name	Formula	Copies
CD	Cadmium ion	Cd	16

Water and common crystallization additives (SO4) are not listed.

Primary citation

Crystal structure of the signal sequence binding subunit of the signal recognition particle. Keenan, R.J., Freymann, D.M., Walter, P. et al. Cell (1998) 94:181-191. DOI 10.1016/S0092-8674(00)81418-X · PubMed

Other PDB entries of the same protein (UniProt O07347 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1LS1 1.1 Å, T. aquaticus Ffh NG Domain at 1.1A Resolution
2J45 1.14 Å, Water structure of T. Aquaticus Ffh NG Domain At 1.1A Resolution
2J46 1.14 Å, Water structure of T. Aquaticus Ffh NG Domain At 1.1A Resolution
2C04 1.15 Å, GMPPCP complex of SRP GTPase Ffh NG Domain at ultra-high resolution
2C03 1.24 Å, GDP complex of srp gtpase ffh ng domain
1JPN 1.9 Å, GMPPNP Complex of SRP GTPase NG Domain
1RJ9 1.9 Å, Structure of the heterodimer of the conserved GTPase domains of the Signal Recognition…
2J7P 1.97 Å, GMPPNP-stabilized NG domain complex of the SRP GTPases Ffh and FtsY
2NG1 2.02 Å, N and gtpase domains of the signal sequence recognition protein ffh from thermus aquaticus
1NG1 2.03 Å, N and gtpase domains of the signal sequence recognition protein ffh from thermus aquaticus
1FFH 2.05 Å, N and gtpase domains of the signal sequence recognition protein ffh from thermus aquaticus
1OKK 2.05 Å, Homo-heterodimeric complex of the srp gtpases

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