5BSA

Structure of histone H3/H4 in complex with Spt2

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	0000786	cellular_component	nucleosome
B	0003677	molecular_function	DNA binding
B	0030527	molecular_function	structural constituent of chromatin
B	0046982	molecular_function	protein heterodimerization activity
C	0000786	cellular_component	nucleosome
C	0003677	molecular_function	DNA binding
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0005694	cellular_component	chromosome
C	0006334	biological_process	nucleosome assembly
C	0030527	molecular_function	structural constituent of chromatin
C	0046982	molecular_function	protein heterodimerization activity
D	0000786	cellular_component	nucleosome
D	0003677	molecular_function	DNA binding
D	0005515	molecular_function	protein binding
D	0005634	cellular_component	nucleus
D	0005694	cellular_component	chromosome
D	0006334	biological_process	nucleosome assembly
D	0030527	molecular_function	structural constituent of chromatin
D	0046982	molecular_function	protein heterodimerization activity

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
C	GLY14-HIS18

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

Chain	Residue	Details
A	PRO66-ILE74

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

Chain	Residue	Details
E	LYS582
F	LYS582

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site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648

Chain	Residue	Details
E	SER599
F	SER599
A	LYS64
B	LYS27
B	LYS36
B	LYS64

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site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate => ECO:0000250|UniProtKB:P62805

Chain	Residue	Details
C	ARG3
D	ARG3

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site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: N6-lactoyllysine; alternate => ECO:0000250|UniProtKB:P62805

Chain	Residue	Details
C	LYS5
D	LYS5

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site_id	SWS_FT_FI5
Number of Residues	8
Details	MOD_RES: N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805

Chain	Residue	Details
C	LYS8
C	LYS16
C	LYS44
C	LYS79
D	LYS8
D	LYS16
D	LYS44
D	LYS79

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:P62805

Chain	Residue	Details
C	LYS12
C	LYS20
D	LYS12
D	LYS20

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62805

Chain	Residue	Details
C	LYS31
C	LYS91
D	LYS31
D	LYS91

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphoserine; by PAK2 => ECO:0000250|UniProtKB:P62805

Chain	Residue	Details
C	SER47
D	SER47
B	THR80
B	THR107

---

site_id	SWS_FT_FI9
Number of Residues	4
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P62805

Chain	Residue	Details
C	TYR51
C	TYR88
D	TYR51
D	TYR88

---

site_id	SWS_FT_FI10
Number of Residues	2
Details	MOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805

Chain	Residue	Details
C	LYS59
D	LYS59

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site_id	SWS_FT_FI11
Number of Residues	2
Details	MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P62805

Chain	Residue	Details
C	LYS77
D	LYS77

---

site_id	SWS_FT_FI12
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate => ECO:0000250|UniProtKB:P62805

Chain	Residue	Details
C	LYS31
D	LYS31

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site_id	SWS_FT_FI13
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62805

Chain	Residue	Details
C	LYS91
D	LYS91

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