1tnz

X-ray diffraction
2.9Å resolution

Rat Protein Geranylgeranyltransferase Type-I Complexed with a GGPP analog and a RRCVLL Peptide Derived from Cdc42 splice isoform-2

Released:

Function and Biology Details

Reactions catalysed:
Farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate
Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha Chains: A, C, E, G, I, K
Molecule details ›
Chains: A, C, E, G, I, K
Length: 377 amino acids
Theoretical weight: 44.1 KDa
Source organism: Rattus norvegicus
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q04631 (Residues: 1-377; Coverage: 100%)
Gene name: Fnta
Sequence domains: Protein prenyltransferase alpha subunit repeat
Structure domains: Protein prenylyltransferase
Geranylgeranyl transferase type-1 subunit beta Chains: B, D, F, H, J, L
Molecule details ›
Chains: B, D, F, H, J, L
Length: 377 amino acids
Theoretical weight: 42.47 KDa
Source organism: Rattus norvegicus
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P53610 (Residues: 1-377; Coverage: 100%)
Gene name: Pggt1b
Sequence domains: Prenyltransferase and squalene oxidase repeat
Structure domains: Glycosyltransferase
Cell division control protein 42 homolog (Cdc42) Chains: M, N, O, P, Q, R
Molecule details ›
Chains: M, N, O, P, Q, R
Length: 6 amino acids
Theoretical weight: 761 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: C2
Unit cell:
a: 271.262Å b: 266.922Å c: 185.75Å
α: 90° β: 131.91° γ: 90°
R-values:
R R work R free
0.199 0.199 0.218
Expression systems:
  • Spodoptera frugiperda
  • Not provided