Crystal Structure of IbpAFic2-H3717A in complex with adenylylated Cdc42. Determined by X-ray diffraction at 2.3 Å resolution. Released 20 Feb 2013.
Explore 4ITR in 3D Show helices and sheets RCSB PDB PDBe
4ITR contains 60 α-helices and 24 β-strands across 4 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3499-3511 | 13 | |
| α-helix | 3513 | 1 | |
| α-helix | 3514-3518 | 5 | |
| α-helix | 3521-3532 | 12 | |
| α-helix | 3537-3543 | 7 | |
| α-helix | 3549-3568 | 20 | |
| α-helix | 3574-3585 | 12 | |
| α-helix | 3593-3594 | 2 | |
| α-helix | 3596-3609 | 14 | |
| α-helix | 3612-3616 | 5 | |
| α-helix | 3618-3635 | 18 | |
| α-helix | 3642-3651 | 10 | |
| β-strand | 3663 | 1 | 1 |
| β-strand | 3668-3669 | 2 | 2 |
| β-strand | 3673 | 1 | 3 |
| α-helix | 3678-3697 | 20 | |
| α-helix | 3702-3716 | 15 | |
| β-strand | 3719 | 1 | 1 |
| α-helix | 3723-3737 | 15 | |
| α-helix | 3740-3743 | 4 | |
| α-helix | 3751-3753 | 3 | |
| β-strand | 3757 | 1 | 3 |
| α-helix | 3767-3779 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3499-3511 | 13 | |
| α-helix | 3513 | 1 | |
| α-helix | 3514-3518 | 5 | |
| α-helix | 3521-3532 | 12 | |
| α-helix | 3537-3543 | 7 | |
| α-helix | 3549-3568 | 20 | |
| α-helix | 3574-3586 | 13 | |
| α-helix | 3593-3595 | 3 | |
| α-helix | 3596-3609 | 14 | |
| α-helix | 3612-3616 | 5 | |
| α-helix | 3618-3635 | 18 | |
| α-helix | 3642-3651 | 10 | |
| β-strand | 3663 | 1 | 4 |
| β-strand | 3668-3669 | 2 | 5 |
| β-strand | 3673 | 1 | 6 |
| α-helix | 3678-3697 | 20 | |
| α-helix | 3702-3716 | 15 | |
| β-strand | 3719 | 1 | 4 |
| α-helix | 3723-3737 | 15 | |
| α-helix | 3740-3743 | 4 | |
| α-helix | 3751-3753 | 3 | |
| β-strand | 3757 | 1 | 6 |
| α-helix | 3767-3779 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-10 | 7 | 7 |
| α-helix | 16-25 | 10 | |
| β-strand | 33-34 | 2 | 5 |
| α-helix | 37-39 | 3 | |
| β-strand | 40-46 | 7 | 7 |
| β-strand | 49-56 | 8 | 7 |
| α-helix | 62-64 | 3 | |
| α-helix | 68-71 | 4 | |
| β-strand | 77-83 | 7 | 7 |
| α-helix | 87-92 | 6 | |
| α-helix | 93-97 | 5 | |
| α-helix | 98-104 | 7 | |
| β-strand | 110-115 | 6 | 7 |
| α-helix | 117-121 | 5 | |
| α-helix | 123-131 | 9 | |
| α-helix | 136-138 | 3 | |
| α-helix | 139-148 | 10 | |
| β-strand | 154-156 | 3 | 7 |
| α-helix | 165-177 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-10 | 7 | 8 |
| α-helix | 16-25 | 10 | |
| β-strand | 33-34 | 2 | 2 |
| α-helix | 37-39 | 3 | |
| β-strand | 40-46 | 7 | 8 |
| β-strand | 49-56 | 8 | 8 |
| α-helix | 62-64 | 3 | |
| α-helix | 68-71 | 4 | |
| β-strand | 77-83 | 7 | 8 |
| α-helix | 87-92 | 6 | |
| α-helix | 93-97 | 5 | |
| α-helix | 98-104 | 7 | |
| β-strand | 110-115 | 6 | 8 |
| α-helix | 117-121 | 5 | |
| α-helix | 123-130 | 8 | |
| α-helix | 136-138 | 3 | |
| α-helix | 139-148 | 10 | |
| β-strand | 154-156 | 3 | 8 |
| α-helix | 165-176 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Adenosine monophosphate-protein transferase and cysteine protease IbpA | A, B | protein | 316 | Haemophilus somnus | Q06277 |
| Cell division control protein 42 homolog | C, D | protein | 191 | Homo sapiens | P60953 (AlphaFold model) |
>4ITR_1 Adenosine monophosphate-protein transferase and cysteine protease IbpA (chains A, B) DETANKVNYQDLEDNLNLKGLISLEDDRNANFESNVLKNEKFLDEAREISKKSIPEATVK QMSHLPEFDDILTEGAKKVESRINKAITFRPSVEEFSEIQDLVKTLPKTKVIEDLSTKTN EITEALAATSKTIQRTPELKEQLKTAIEDFLQNSQGKPLTVQMIENLNHGLRPDEGEGRL LYKKENLTKENAVFSSPEAAKIQLAETVDFINRAKNEGIEPSVVGALVYQRLIAYAPFAE GNGRMARVIVNKILLDAGYPAFTKFSDEFEPQIIPQTKASTKSATSSEVVVEFLKELAKK GSKEDNEQNLEKTDRT
>4ITR_2 Cell division control protein 42 homolog (chains C, D) MQTIKCVVVGDGAVGKTCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPYTLGLFDTAG QEDYDRLRPLSYPQTDVFLVCFSVVSPSSFENVKEKWVPEITHHCPKTPFLLVGTQIDLR DDPSTIEKLAKNKQKPITPETAEKLARDLKAVKYVECSALTQKGLKNVFDEAILAALEPP EPKKSRRCVLL
| ID | Name | Formula | Copies |
|---|---|---|---|
| AMP | Adenosine monophosphate | C10 H14 N5 O7 P | 2 |
| MG | Magnesium ion | Mg | 2 |
| GDP | Guanosine-5'-diphosphate | C10 H15 N5 O11 P2 | 2 |
Water and common crystallization additives (SO4) are not listed.
Structural basis of Fic-mediated adenylylation. Xiao, J., Worby, C.A., Mattoo, S. et al. Nat Struct Mol Biol (2010) 17:1004-1010. DOI 10.1038/nsmb.1867 · PubMed
Other PDB entries of the same protein (UniProt Q06277), best resolution first:
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