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5BNV

Crystal structure of Human MCM2 HBD chaperoning a histone H3-H4 tetramer

Functional Information from GO Data
ChainGOidnamespacecontents
A0000786cellular_componentnucleosome
A0003677molecular_functionDNA binding
A0030527molecular_functionstructural constituent of chromatin
A0046982molecular_functionprotein heterodimerization activity
B0000781cellular_componentchromosome, telomeric region
B0000786cellular_componentnucleosome
B0003677molecular_functionDNA binding
B0003723molecular_functionRNA binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005694cellular_componentchromosome
B0006325biological_processchromatin organization
B0006334biological_processnucleosome assembly
B0016020cellular_componentmembrane
B0030527molecular_functionstructural constituent of chromatin
B0032200biological_processtelomere organization
B0032991cellular_componentprotein-containing complex
B0043505cellular_componentCENP-A containing nucleosome
B0045653biological_processnegative regulation of megakaryocyte differentiation
B0046982molecular_functionprotein heterodimerization activity
B0061644biological_processprotein localization to CENP-A containing chromatin
B0070062cellular_componentextracellular exosome
C0003677molecular_functionDNA binding
C0005524molecular_functionATP binding
C0005634cellular_componentnucleus
C0006270biological_processDNA replication initiation
C0042555cellular_componentMCM complex
C1905775biological_processnegative regulation of DNA helicase activity
D0000786cellular_componentnucleosome
D0003677molecular_functionDNA binding
D0030527molecular_functionstructural constituent of chromatin
D0046982molecular_functionprotein heterodimerization activity
E0000781cellular_componentchromosome, telomeric region
E0000786cellular_componentnucleosome
E0003677molecular_functionDNA binding
E0003723molecular_functionRNA binding
E0005515molecular_functionprotein binding
E0005576cellular_componentextracellular region
E0005634cellular_componentnucleus
E0005654cellular_componentnucleoplasm
E0005694cellular_componentchromosome
E0006325biological_processchromatin organization
E0006334biological_processnucleosome assembly
E0016020cellular_componentmembrane
E0030527molecular_functionstructural constituent of chromatin
E0032200biological_processtelomere organization
E0032991cellular_componentprotein-containing complex
E0043505cellular_componentCENP-A containing nucleosome
E0045653biological_processnegative regulation of megakaryocyte differentiation
E0046982molecular_functionprotein heterodimerization activity
E0061644biological_processprotein localization to CENP-A containing chromatin
E0070062cellular_componentextracellular exosome
F0003677molecular_functionDNA binding
F0005524molecular_functionATP binding
F0005634cellular_componentnucleus
F0006270biological_processDNA replication initiation
F0042555cellular_componentMCM complex
F1905775biological_processnegative regulation of DNA helicase activity
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue PO4 B 201
ChainResidue
BARG35
FARG79

site_idAC2
Number of Residues1
Detailsbinding site for residue PO4 B 202
ChainResidue
BARG23

site_idAC3
Number of Residues4
Detailsbinding site for residue PO4 E 201
ChainResidue
DARG63
ETHR30
EPRO32
EARG36

Functional Information from PROSITE/UniProt
site_idPS00047
Number of Residues5
DetailsHISTONE_H4 Histone H4 signature. GAKRH
ChainResidueDetails
BGLY14-HIS18

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
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
FSER108
CSER108

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:17967882
ChainResidueDetails
BSER1
ESER1

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate => ECO:0000250|UniProtKB:P62806
ChainResidueDetails
BARG3
EARG3

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732
ChainResidueDetails
BLYS5
ELYS5

site_idSWS_FT_FI5
Number of Residues6
DetailsMOD_RES: N6-propionyllysine; alternate => ECO:0000269|PubMed:17267393
ChainResidueDetails
BLYS8
BLYS16
BLYS44
ELYS8
ELYS16
ELYS44

site_idSWS_FT_FI6
Number of Residues8
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435
ChainResidueDetails
BLYS12
BLYS31
BLYS77
BLYS91
ELYS12
ELYS31
ELYS77
ELYS91

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:12086618, ECO:0000269|PubMed:15964846, ECO:0000269|PubMed:17967882, ECO:0000269|PubMed:27338793
ChainResidueDetails
BLYS20
ELYS20

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PAK2 => ECO:0000269|PubMed:21724829, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
BSER47
ESER47

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:20068231
ChainResidueDetails
BTYR51
ETYR51

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297
ChainResidueDetails
BLYS59
ELYS59

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62806
ChainResidueDetails
BLYS79
ELYS79

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P62806
ChainResidueDetails
BTHR80
ETHR80

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:24275569
ChainResidueDetails
BTYR88
ETYR88

site_idSWS_FT_FI14
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25218447
ChainResidueDetails
BLYS12
ELYS12

site_idSWS_FT_FI15
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:19818714
ChainResidueDetails
BLYS91
ELYS91

site_idSWS_FT_FI16
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
ChainResidueDetails
BLYS20
BLYS59
BLYS79
ELYS20
ELYS59
ELYS79

site_idSWS_FT_FI17
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate => ECO:0000269|PubMed:30886146
ChainResidueDetails
BLYS31
ELYS31

225681

PDB entries from 2024-10-02

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