1CTQ: P21RAS

Structure of P21RAS in complex with gppnhp at 100 K. Determined by X-ray diffraction at 1.26 Å resolution. Released 15 Nov 1999.

Method: X-ray diffraction
Resolution: 1.26 Å
Organism: Homo sapiens
Chains: 1
Atoms: 1,655
Mol. weight: 19.42 kDa
Ligands: MG, GNP
Released: 15 Nov 1999

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

Secondary structure: helices and β-sheets

1CTQ contains 7 α-helices and 6 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: 7 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	2-10	9	1
α-helix	16-25	10
β-strand	37-46	10	1
β-strand	49-58	10	1
α-helix	62-64	3
α-helix	65-74	10
β-strand	77-83	7	1
α-helix	87-91	5
α-helix	93-104	12
β-strand	111-116	6	1
α-helix	127-137	11
β-strand	141-143	3	1
α-helix	152-164	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein (transforming protein P21/H-ras-1)	A	protein	166	Homo sapiens	P01112 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1CTQ_1 PROTEIN (TRANSFORMING PROTEIN P21/H-RAS-1) (chains A)
MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAG
QEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDL
AARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQH

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	1
GNP	Phosphoaminophosphonic acid-guanylate ester	C10 H17 N6 O13 P3	1

Primary citation

The pre-hydrolysis state of p21(ras) in complex with GTP: new insights into the role of water molecules in the GTP hydrolysis reaction of ras-like proteins. Scheidig, A.J., Burmester, C., Goody, R.S. Structure (1999) 7:1311-1324. DOI 10.1016/S0969-2126(00)80021-0 · PubMed

Other PDB entries of the same protein (UniProt P01112 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2CE2 1.0 Å, Crystal structure analysis of a fluorescent form of H-ras P21 in complex with GDP
2EVW 1.05 Å, Crystal structure analysis of a fluorescent form of H-Ras p21 in complex with R-caged GTP
24SQ 1.08 Å, Human HRAS WT (GDP-bound) in complex with macrocyclic peptide inhibitor AP6296
8TBG 1.2 Å, Tricomplex of RMC-7977, HRAS WT, and CypA
2CLD 1.22 Å, Crystal structure analysis of a fluorescent form of H-ras P21 in complex with GDP (2)
2CL6 1.24 Å, Crystal structure analysis of a fluorescent form of H-ras P21 in complex with S-caged GTP
2CL7 1.25 Å, Crystal structure analysis of a fluorescent form of H-ras P21 in complex with GTP
5WDQ 1.25 Å, H-Ras mutant L120A bound to GMP-PNP at 100K
2CLC 1.3 Å, Crystal structure analysis of a fluorescent form of H-ras P21 in complex with GTP (2)
3K8Y 1.3 Å, Allosteric modulation of H-Ras GTPase
3OIW 1.3 Å, H-RasG12V with allosteric switch in the "on" state
3TGP 1.31 Å, Room temperature H-ras

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