2NG1: Signal sequence recognition protein ffh

N and gtpase domains of the signal sequence recognition protein ffh from thermus aquaticus. Determined by X-ray diffraction at 2.02 Å resolution. Released 30 Jul 1999.

Method: X-ray diffraction
Resolution: 2.02 Å
Organism: Thermus aquaticus
Chains: 1
Atoms: 2,375
Mol. weight: 32.85 kDa
Ligands: DIO, GDP
Released: 30 Jul 1999

Explore 2NG1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2NG1 contains 16 α-helices and 8 β-strands across 1 chain. 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: 16 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	3-14	12
α-helix	24-39	16
α-helix	45-61	17
α-helix	64-66	3
α-helix	70-86	17
β-strand	99-105	7	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	159-160	2
α-helix	165-179	15
β-strand	183-187	5	1
α-helix	196-209	14
β-strand	213-219	7	1
α-helix	220-225	6
α-helix	228-236	9
β-strand	241-245	5	1
α-helix	247-249	3
α-helix	254-262	9
β-strand	267-271	5	1
α-helix	276-278	3
β-strand	279-281	3	1
α-helix	284-291	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Signal sequence recognition protein ffh	A	protein	293	Thermus aquaticus	O07347 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2NG1_1 SIGNAL SEQUENCE RECOGNITION PROTEIN FFH (chains A)
FQQLSARLQEAIGRLRGRGRITEEDLKATLREIRRALMDADVNLEVTRDFVERVREEALG
KQVLESLTPAEVILATVYEALKEALGGEARLPVLKDRNLWFLVGLQGSGKTTTAAKLALY
YKGKGRRPLLVAADTQRPAAREQLRLLGEKVGVPVLEVMDGESPESIRRRVEEKARLEAR
DLILVDTAGRLQIDEPLMGELARLKEVLGPDEVLLVLDAMTGQEALSVARAFDEKVGVTG
LVLTKLDGDARGGAALSARHVTGKPIYFAGVSEKPEGLEPFYPERLAGRILGM

Ligands and cofactors

ID	Name	Formula	Copies
DIO	1,4-diethylene dioxide	C4 H8 O2	1
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	1

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

Primary citation

Functional changes in the structure of the SRP GTPase on binding GDP and Mg2+GDP. Freymann, D.M., Keenan, R.J., Stroud, R.M. et al. Nat Struct Biol (1999) 6:793-801. DOI 10.1038/11572 · 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
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
1O87 2.1 Å, A new MgGDP complex of the Ffh NG domain

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