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Fully refined crystal structure of the haloarcula marismortui large ribosomal subunit at 2.4 ångström resolution

Analyse Fully refined crystal structure of the haloarcula marismortui large ribosomal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1JJ2
Type
protein + RNA
Length
6,577 residues
Chains
30
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
23S rRNA; 5S rRNA; Ribosomal protein L2; Ribosomal protein L3; Ribosomal protein L4…
UniProt
P20276, P20279, P12735, P14124, P14135, P12743, P15825, P29198, P22450, P12737, P14123, P12733, P14119, P12734, P10970, P12732, P10972, P14116, P10971, P14121, P18138, P12736, P32410, P22452, P32411
Ligands
MG, NA, CD, K, CL
Pockets
20 · best druggability 0.90

Structure

x-ray diffraction · 30 distinct chains · 29% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
023S rRNArna2754——
95S rRNArna122——
ARibosomal protein L2protein23712% helix, 24% strandP20276
BRibosomal protein L3protein33714% helix, 32% strandP20279
CRibosomal protein L4protein24632% helix, 14% strandP12735
DRibosomal protein L5protein14024% helix, 21% strandP14124
ERibosomal protein L6protein17222% helix, 41% strandP14135
FRibosomal protein L7AEprotein11947% helix, 13% strandP12743
GRibosomal protein L10protein2979% helix, 0% strandP15825
HRibosomal protein L10Eprotein15615% helix, 28% strand—
IRibosomal protein L13protein14240% helix, 15% strandP29198
JRibosomal protein L14protein1325% helix, 39% strandP22450
KRibosomal protein L15protein14519% helix, 16% strandP12737
LRibosomal protein L15Eprotein19432% helix, 16% strand—
MRibosomal protein L18protein18639% helix, 13% strandP14123
NRibosomal protein L18Eprotein11546% helix, 23% strandP12733
ORibosomal protein L19Eprotein14362% helix, 4% strandP14119
PRibosomal protein L21Eprotein9511% helix, 32% strandP12734
QRibosomal protein L22protein15035% helix, 32% strandP10970
RRibosomal protein L23protein8135% helix, 31% strandP12732
SRibosomal protein L24protein11929% helix, 29% strandP10972
TRibosomal protein L24Eprotein5321% helix, 19% strandP14116
URibosomal protein L29protein6574% helix, 0% strandP10971
VRibosomal protein L30protein15440% helix, 14% strandP14121
WRibosomal protein L31Eprotein8241% helix, 28% strandP18138
XRibosomal protein L32Eprotein14223% helix, 12% strandP12736
YRibosomal protein L37AEprotein7337% helix, 18% strand—
ZRibosomal protein L37Eprotein5613% helix, 16% strandP32410
1Ribosomal protein L39Eprotein4643% helix, 0% strandP22452
2Ribosomal protein L44Eprotein9214% helix, 33% strandP32411

Ligands and binding sites

  • MG · Magnesium ion · metal · 117 copies · chains 0, A, C, B, Z, L, R, Q, V, 9, 1, X, 2, O, Y, T, J, S
  • NA · Sodium ion · metal · 86 copies · chains 0, K, B, 1, X, Q, 9, I, C, L, 2, D, A, H, P, R, S
  • CD · Cadmium ion · metal · 5 copies · chains N, T, Y, Z, 2
  • K · Potassium ion · metal · 2 copies · chains 0, L
  • CL · Chloride ion · ion · 22 copies · chains 0, 1, P, J, K, I, X, A, B, E, L, D, M, N, Q, 2

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110560.900.9294MG, NA
29660.880.91119MG, CL
311020.870.8993NA
46410.870.9387NA
59390.870.8989empty

Interfaces

53 interfaces between chains.

  • 0–B · 7376 Ų buried · 231 hydrogen bonds · protein-nucleic
  • 0–L · 6931 Ų buried · 177 hydrogen bonds · protein-nucleic
  • 0–A · 6305 Ų buried · 180 hydrogen bonds · protein-nucleic
  • 0–C · 5595 Ų buried · 129 hydrogen bonds · protein-nucleic
  • 0–O · 4371 Ų buried · 122 hydrogen bonds · protein-nucleic

Compared structures

  • 1JJ2 · Fully Refined Crystal Structure of the Haloarcula marismortui Large Ribosomal Subunit at… · the same entry in another collection · chain H against H, TM-score 1.00

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