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6XWS

Crystal Structure of Drosophila CAL1 1-160 bound to CENP-A/H4

Functional Information from GO Data
ChainGOidnamespacecontents
A0000278biological_processmitotic cell cycle
A0000775cellular_componentchromosome, centromeric region
A0000776cellular_componentkinetochore
A0000779cellular_componentcondensed chromosome, centromeric region
A0000786cellular_componentnucleosome
A0000939cellular_componentinner kinetochore
A0003677molecular_functionDNA binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005694cellular_componentchromosome
A0007059biological_processchromosome segregation
A0007080biological_processmitotic metaphase chromosome alignment
A0030527molecular_functionstructural constituent of chromatin
A0031507biological_processheterochromatin formation
A0043505cellular_componentCENP-A containing nucleosome
A0046982molecular_functionprotein heterodimerization activity
A0051225biological_processspindle assembly
A0051382biological_processkinetochore assembly
A0051383biological_processkinetochore organization
B0000228cellular_componentnuclear chromosome
B0000786cellular_componentnucleosome
B0003676molecular_functionnucleic acid binding
B0003677molecular_functionDNA binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005694cellular_componentchromosome
B0006334biological_processnucleosome assembly
B0030527molecular_functionstructural constituent of chromatin
B0035059cellular_componentRCAF complex
B0046982molecular_functionprotein heterodimerization activity
Functional Information from PROSITE/UniProt
site_idPS00047
Number of Residues5
DetailsHISTONE_H4 Histone H4 signature. GAKRH
ChainResidueDetails
BGLY15-HIS19

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsDNA_BIND:
ChainResidueDetails
BLYS17-LYS21
ASER-25
ASER-23

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:16230526
ChainResidueDetails
BLYS6
BLYS13

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: N6-succinyllysine => ECO:0000269|PubMed:22389435
ChainResidueDetails
BLYS32
BLYS78
BLYS80
BLYS92

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:18327897
ChainResidueDetails
BTHR81
BTHR83

222926

PDB entries from 2024-07-24

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