2C03: GDP complex of srp gtpase ffh ng domain

GDP complex of srp gtpase ffh ng domain. Determined by X-ray diffraction at 1.24 Å resolution. Released 13 Feb 2007.

Method: X-ray diffraction
Resolution: 1.24 Å
Organism: THERMUS AQUATICUS
Chains: 2
Atoms: 6,700
Mol. weight: 67.51 kDa
Ligands: GDP, DIO
Released: 13 Feb 2007

Explore 2C03 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2C03 contains 27 α-helices and 16 β-strands across 2 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: 13 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	3-14	12
α-helix	24-40	17
α-helix	45-61	17
α-helix	70-85	16
α-helix	93-95	3
β-strand	100-104	5	1
α-helix	111-124	14
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	225-236	12
β-strand	241-245	5	1
α-helix	254-263	10
β-strand	267-271	5	1
β-strand	279-281	3	1
α-helix	284-291	8

Chain B: 14 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	3-14	12
α-helix	24-40	17
α-helix	45-61	17
α-helix	64-66	3
α-helix	70-85	16
α-helix	93-95	3
β-strand	100-104	5	2
α-helix	111-124	14
β-strand	129-133	5	2
α-helix	139-152	14
β-strand	156-158	3	2
α-helix	159-160	2
α-helix	165-178	14
β-strand	183-187	5	2
α-helix	196-209	14
β-strand	213-219	7	2
α-helix	225-236	12
β-strand	241-245	5	2
α-helix	254-263	10
β-strand	267-271	5	2
β-strand	279-281	3	2
α-helix	284-291	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Signal recognition particle protein	A, B	protein	297	THERMUS AQUATICUS	O07347 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>2C03_1 SIGNAL RECOGNITION PARTICLE PROTEIN (chains A, B)
MFQQLSARLQEAIGRLRGRGRITEEDLKATLREIRRALMDADVNLEVTRDFVERVREEAL
GKQVLESLTPAEVILATVYEALKEALGGEARLPVLKDRNLWFLVGLQGSGKTTTAAKLAL
YYKGKGRRPLLVAADTQRPAAREQLRLLGEKVGVPVLEVMDGESPESIRRRVEEKARLEA
RDLILVDTAGRLQIDEPLMGELARLKEVLGPDEVLLVLDAMTGQEALSVARAFDEKVGVT
GLVLTKLDGDARGGAALSARHVTGKPIYFAGVSEKPEGLEPFYPERLAGRILGMGDV

Ligands and cofactors

ID	Name	Formula	Copies
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	2
DIO	1,4-diethylene dioxide	C4 H8 O2	14

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

Primary citation

Nucleotide-Binding Flexibility in Ultrahigh-Resolution Structures of the Srp Gtpase Ffh. Ramirez, U.D., Focia, P.J., Freymann, D.M. Acta Crystallogr D Biol Crystallogr (2008) 64:1043. DOI 10.1107/S090744490802444X · 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
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
1O87 2.1 Å, A new MgGDP complex of the Ffh NG domain

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