Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5BO0

Crystal structure of Human MCM2 HBD and ASF1b chaperoning a histone H3.2-H4 dimer

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000786	cellular_component	nucleosome
A	0003677	molecular_function	DNA binding
A	0030527	molecular_function	structural constituent of chromatin
A	0046982	molecular_function	protein heterodimerization activity
B	0000781	cellular_component	chromosome, telomeric region
B	0000786	cellular_component	nucleosome
B	0003677	molecular_function	DNA binding
B	0003723	molecular_function	RNA binding
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0005694	cellular_component	chromosome
B	0006325	biological_process	chromatin organization
B	0006334	biological_process	nucleosome assembly
B	0016020	cellular_component	membrane
B	0030527	molecular_function	structural constituent of chromatin
B	0032200	biological_process	telomere organization
B	0032991	cellular_component	protein-containing complex
B	0043505	cellular_component	CENP-A containing nucleosome
B	0045653	biological_process	negative regulation of megakaryocyte differentiation
B	0046982	molecular_function	protein heterodimerization activity
B	0061644	biological_process	protein localization to CENP-A containing chromatin
B	0070062	cellular_component	extracellular exosome
C	0003677	molecular_function	DNA binding
C	0005524	molecular_function	ATP binding
C	0005634	cellular_component	nucleus
C	0006270	biological_process	DNA replication initiation
C	0042555	cellular_component	MCM complex
C	1905775	biological_process	negative regulation of DNA helicase activity
D	0005634	cellular_component	nucleus
D	0006325	biological_process	chromatin organization

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	binding site for residue GOL B 201

Chain	Residue
A	ILE62
A	ARG63
B	ILE29
B	THR30
B	ALA33
B	ARG36
D	ARG69

Functional Information from PROSITE/UniProt

site_id	PS00047
Number of Residues	5
Details	HISTONE_H4 Histone H4 signature. GAKRH

Chain	Residue	Details
B	GLY14-HIS18

site_id	PS00959
Number of Residues	9
Details	HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI

Chain	Residue	Details
A	PRO66-ILE74

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	MOD_RES: Phosphoserine; by ATR => ECO:0000269\|PubMed:15210935, ECO:0000269\|PubMed:16899510, ECO:0007744\|PubMed:17525332, ECO:0007744\|PubMed:19690332, ECO:0007744\|PubMed:20068231

Chain	Residue	Details
C	SER108

site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000269\|PubMed:17967882

Chain	Residue	Details
B	SER1

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate => ECO:0000250\|UniProtKB:P62806

Chain	Residue	Details
B	ARG3

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: N6-lactoyllysine; alternate => ECO:0000269\|PubMed:31645732

Chain	Residue	Details
B	LYS5

site_id	SWS_FT_FI5
Number of Residues	3
Details	MOD_RES: N6-propionyllysine; alternate => ECO:0000269\|PubMed:17267393

Chain	Residue	Details
B	LYS8
B	LYS16
B	LYS44

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000269\|PubMed:22389435

Chain	Residue	Details
B	LYS91
B	LYS12
B	LYS31
B	LYS77

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: N6-methyllysine; alternate => ECO:0000269\|PubMed:12086618, ECO:0000269\|PubMed:15964846, ECO:0000269\|PubMed:17967882, ECO:0000269\|PubMed:27338793

Chain	Residue	Details
B	LYS20

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_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

Chain	Residue	Details
B	SER47

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0007744\|PubMed:15592455, ECO:0007744\|PubMed:20068231

Chain	Residue	Details
B	TYR51

site_id	SWS_FT_FI10
Number of Residues	1
Details	MOD_RES: N6-glutaryllysine; alternate => ECO:0000269\|PubMed:31542297

Chain	Residue	Details
B	LYS59

site_id	SWS_FT_FI11
Number of Residues	1
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250\|UniProtKB:P62806

Chain	Residue	Details
B	LYS79

site_id	SWS_FT_FI12
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0000250\|UniProtKB:P62806

Chain	Residue	Details
B	THR80

site_id	SWS_FT_FI13
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0007744\|PubMed:24275569

Chain	Residue	Details
B	TYR88

site_id	SWS_FT_FI14
Number of Residues	1
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744\|PubMed:25218447

Chain	Residue	Details
B	LYS12

site_id	SWS_FT_FI15
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269\|PubMed:19818714

Chain	Residue	Details
B	LYS91

site_id	SWS_FT_FI16
Number of Residues	3
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744\|PubMed:28112733

Chain	Residue	Details
B	LYS20
B	LYS59
B	LYS79

site_id	SWS_FT_FI17
Number of Residues	1
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate => ECO:0000269\|PubMed:30886146

Chain	Residue	Details
B	LYS31

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)