Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4UUZ

MCM2-histone complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000785cellular_componentchromatin
A0000786cellular_componentnucleosome
A0003677molecular_functionDNA binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005694cellular_componentchromosome
A0005700cellular_componentpolytene chromosome
A0006334biological_processnucleosome assembly
A0030527molecular_functionstructural constituent of chromatin
A0031492molecular_functionnucleosomal DNA binding
A0035059cellular_componentRCAF complex
A0046982molecular_functionprotein heterodimerization activity
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
C0003677molecular_functionDNA binding
C0005524molecular_functionATP binding
C0005634cellular_componentnucleus
C0006270biological_processDNA replication initiation
C0042555cellular_componentMCM complex
C1905775biological_processnegative regulation of DNA helicase activity
Functional Information from PROSITE/UniProt
site_idPS00322
Number of Residues7
DetailsHISTONE_H3_1 Histone H3 signature 1. KAPRKQL
ChainResidueDetails
ALYS14-LEU20

site_idPS00959
Number of Residues9
DetailsHISTONE_H3_2 Histone H3 signature 2. PFqRLVREI
ChainResidueDetails
APRO66-ILE74

site_idPS00047
Number of Residues5
DetailsHISTONE_H4 Histone H4 signature. GAKRH
ChainResidueDetails
BGLY14-HIS18

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphoserine; by ATR => ECO:0000269|PubMed:15210935, ECO:0000269|PubMed:16899510, ECO:0007744|PubMed:17525332, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231
ChainResidueDetails
CSER108

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:24275569
ChainResidueDetails
CTYR137
BLYS12

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: N6-succinyllysine => ECO:0000269|PubMed:22389435
ChainResidueDetails
ALYS37
BLYS31
BLYS77
BLYS79
BLYS91

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:18327897
ChainResidueDetails
BTHR80
BTHR82

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:14732680
ChainResidueDetails
ALYS23
ALYS18

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-succinyllysine => ECO:0000269|PubMed:22389435
ChainResidueDetails
ALYS56

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435
ChainResidueDetails
ALYS79

218500

PDB entries from 2024-04-17

PDB statisticsPDBj update infoContact PDBjnumon