Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6S1R

Structure of fission yeast Mis16 bound to histone H4

Functional Information from GO Data
ChainGOidnamespacecontents
A0000510molecular_functionH3-H4 histone complex chaperone activity
A0000775cellular_componentchromosome, centromeric region
A0000776cellular_componentkinetochore
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005694cellular_componentchromosome
A0005737cellular_componentcytoplasm
A0006325biological_processchromatin organization
A0006338biological_processchromatin remodeling
A0034080biological_processCENP-A containing chromatin assembly
A0042393molecular_functionhistone binding
A0098654cellular_componentCENP-A recruiting complex
A0140463molecular_functionchromatin-protein adaptor activity
B0000786cellular_componentnucleosome
B0003677molecular_functionDNA binding
B0030527molecular_functionstructural constituent of chromatin
B0046982molecular_functionprotein heterodimerization activity
Functional Information from PROSITE/UniProt
site_idPS00047
Number of Residues5
DetailsHISTONE_H4 Histone H4 signature. GAKRH
ChainResidueDetails
BGLY15-HIS19

site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LATGaeDqVICLWDV
ChainResidueDetails
ALEU198-VAL212
ALEU297-LEU311
ALEU341-LEU355

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsDNA_BIND:
ChainResidueDetails
BLYS17-LYS21

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:18257517
ChainResidueDetails
ASER425

237423

PDB entries from 2025-06-11

PDB statisticsPDBj update infoContact PDBjnumon