5BS7

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 PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue SO4 C 201

Chain	Residue
C	ARG39
C	LYS44
E	ASP632
E	SER634

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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: Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5 => ECO:0000250|UniProtKB:Q71DI3

Chain	Residue	Details
A	SER28
B	SER28

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68431

Chain	Residue	Details
A	LYS37
B	LYS37

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3

Chain	Residue	Details
A	TYR41
B	TYR41
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-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228

Chain	Residue	Details
A	LYS56
A	LYS79
B	LYS56
B	LYS79

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q71DI3

Chain	Residue	Details
A	SER57
B	SER57
D	LYS31
D	LYS91

---

site_id	SWS_FT_FI8
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3

Chain	Residue	Details
A	THR80
A	THR107
B	THR80
B	THR107

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P84243

Chain	Residue	Details
A	SER86
B	SER86
D	TYR51
D	TYR88

---

site_id	SWS_FT_FI10
Number of Residues	2
Details	MOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3

Chain	Residue	Details
A	LYS115
B	LYS115

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site_id	SWS_FT_FI11
Number of Residues	2
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3

Chain	Residue	Details
A	LYS122
B	LYS122

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site_id	SWS_FT_FI12
Number of Residues	2
Details	LIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3

Chain	Residue	Details
A	CYS110
B	CYS110

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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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