1AM4: Complex between CDC42HS.GMPPNP and P50 rhogap
Complex between CDC42HS.GMPPNP and P50 rhogap (H. Sapiens). Determined by X-ray diffraction at 2.7 Å resolution. Released 15 Jul 1998.
- Method
- X-ray diffraction
- Resolution
- 2.7 Å
- Organism
- Homo sapiens
- Chains
- 6
- Atoms
- 9,191
- Mol. weight
- 128.78 kDa
- Ligands
- GNP, MG
- Released
- 15 Jul 1998
Explore 1AM4 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
1AM4 contains 72 α-helices and 18 β-strands across 6 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.
Chains A and C: 14 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 49-52 | 4 | |
| α-helix | 64-75 | 12 | |
| α-helix | 87-88 | 2 | |
| α-helix | 90-99 | 10 | |
| α-helix | 116-126 | 11 | |
| α-helix | 135-137 | 3 | |
| α-helix | 138-142 | 5 | |
| α-helix | 144-146 | 3 | |
| α-helix | 152-161 | 10 | |
| α-helix | 165-182 | 18 | |
| α-helix | 185-188 | 4 | |
| α-helix | 192-203 | 12 | |
| α-helix | 218-228 | 11 | |
| α-helix | 230-233 | 4 | |
Chain B: 13 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 49-54 | 6 | |
| α-helix | 64-75 | 12 | |
| α-helix | 87-88 | 2 | |
| α-helix | 90-99 | 10 | |
| α-helix | 116-126 | 11 | |
| α-helix | 137-142 | 6 | |
| α-helix | 144-146 | 3 | |
| α-helix | 152-161 | 10 | |
| α-helix | 165-182 | 18 | |
| α-helix | 185-188 | 4 | |
| α-helix | 192-203 | 12 | |
| α-helix | 218-228 | 11 | |
| α-helix | 230-233 | 4 | |
Chain D: 11 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 503-510 | 8 | 1 |
| α-helix | 516-525 | 10 | |
| β-strand | 541-544 | 4 | 1 |
| β-strand | 551-557 | 7 | 1 |
| α-helix | 562-565 | 4 | |
| α-helix | 569-571 | 3 | |
| β-strand | 578-583 | 6 | 1 |
| α-helix | 588-591 | 4 | |
| α-helix | 593-597 | 5 | |
| α-helix | 598-602 | 5 | |
| β-strand | 610-615 | 6 | 1 |
| α-helix | 618-620 | 3 | |
| α-helix | 623-627 | 5 | |
| α-helix | 636-638 | 3 | |
| α-helix | 643-649 | 7 | |
| β-strand | 651-656 | 6 | 1 |
| α-helix | 665-676 | 12 | |
Chain E: 10 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 503-510 | 8 | 2 |
| α-helix | 516-525 | 10 | |
| β-strand | 541-544 | 4 | 2 |
| β-strand | 551-557 | 7 | 2 |
| α-helix | 563-565 | 3 | |
| α-helix | 569-571 | 3 | |
| β-strand | 578-583 | 6 | 2 |
| α-helix | 588-591 | 4 | |
| α-helix | 593-597 | 5 | |
| α-helix | 598-602 | 5 | |
| β-strand | 610-615 | 6 | 2 |
| α-helix | 618-620 | 3 | |
| α-helix | 623-627 | 5 | |
| α-helix | 643-649 | 7 | |
| β-strand | 651-656 | 6 | 2 |
| α-helix | 665-676 | 12 | |
Chain F: 10 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 503-510 | 8 | 3 |
| α-helix | 516-525 | 10 | |
| β-strand | 541-544 | 4 | 3 |
| β-strand | 551-557 | 7 | 3 |
| α-helix | 562-565 | 4 | |
| α-helix | 568-571 | 4 | |
| β-strand | 578-583 | 6 | 3 |
| α-helix | 588-591 | 4 | |
| α-helix | 593-597 | 5 | |
| α-helix | 598-602 | 5 | |
| β-strand | 610-615 | 6 | 3 |
| α-helix | 618-620 | 3 | |
| α-helix | 623-627 | 5 | |
| α-helix | 643-649 | 7 | |
| β-strand | 651-656 | 6 | 3 |
| α-helix | 665-676 | 12 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| P50-rhogap | A, B, C | protein | 199 | Homo sapiens | Q07960 (AlphaFold model) |
| CDC42HS | D, E, F | protein | 177 | Homo sapiens | P60953 (AlphaFold model) |
Sequence of entity 1 (A, B, C), FASTA
>1AM4_1 P50-RHOGAP (chains A, B, C)
PRPPLPNQQFGVSLQHLQEKNPEQEPIPIVLRETVAYLQAHALTTEGIFRRSANTQVVRE
VQQKYNMGLPVDFDQYNELHLPAVILKTFLRELPEPLLTFDLYPHVVGFLNIDESQRVPA
TLQVLQTLPEENYQVLRFLTAFLVQISAHSDQNKMTNTNLAVVFGPNLLWAKDAAITLKA
INPINTFTKFLLDHQGELF
Sequence of entity 2 (D, E, F), FASTA
>1AM4_2 CDC42HS (chains D, E, F)
PQTIKCVVVGDGAVGKTCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPYTLGLFDTAG
QEDYDRLRPLSYPQTDVFLVCFSVVSPSSFENVKEKWVPEITHHCPKTPFLLVGTQIDLR
DDPSTIEKLAKNKQKPITPETAEKLARDLKAVKYVECSALTQRGLKNVFDEAILAAL
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| GNP | Phosphoaminophosphonic acid-guanylate ester | C10 H17 N6 O13 P3 | 3 |
| MG | Magnesium ion | Mg | 3 |
Primary citation
Crystal structure of a small G protein in complex with the GTPase-activating protein rhoGAP. Rittinger, K., Walker, P.A., Eccleston, J.F. et al. Nature (1997) 388:693-697. DOI 10.1038/41805 · PubMed
Other PDB entries of the same protein (UniProt Q07960 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 1TX4 1.65 Å, RHO/RHOGAP/GDP(DOT)ALF4 complex
- 6R3V 1.75 Å, Crystal Structure of RhoA-GDP-Pi in Complex with RhoGAP
- 1OW3 1.8 Å, Crystal Structure of RhoA.GDP.MgF3-in Complex with RhoGAP
- 2NGR 1.9 Å, Transition state complex for GTP hydrolysis by CDC42: comparisons of the high resolution…
- 7QSC 1.91 Å, Gtpase in complex with GDP.MGF3-
- 1RGP 2.0 Å, Gtpase-activation domain from rhogap
- 1GRN 2.1 Å, Crystal structure of the CDC42/CDC42GAP/ALF3 complex.
- 5M70 2.2 Å, Crystal Structure of human RhoGAP mutated in its arginin finger (R85A) in complex with…
- 7QTM 2.25 Å, Transition state analogue of small G protein in complex with relevant GAP
- 5M6X 2.4 Å, Crystal Structure of human RhoGAP mutated in its arginine finger (R85A) in complex with…
Browse structure collections
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