eF-site ID 4kud-ABCDEFGHIJ
PDB Code 4kud
Chain A, B, C, D, E, F, G, H, I, J

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Title Crystal structure of N-terminal acetylated Sir3 BAH domain D205N mutant in complex with yeast nucleosome core particle
Classification STRUCTURAL PROTEIN/TRANSCRIPTION/DNA
Compound Histone H3
Source Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (SIR3_YEAST)
Sequence A:  PHRYKPGTVALREIRRFQKSTELLIRKLPFQRLVREIAQD
FKTDLRFQSSAIGALQESVEAYLVSLFEDTNLAAIHAKRV
TIQKKDIKLARRLRGE
B:  AKRHRKILRDNIQGITKPAIRRLARRGGVKRISGLIYEEV
RAVLKSFLESVIRDSVTYTEHAKRKTVTSLDVVYALKRQG
RTLYGFGG
C:  QSRSAKAGLTFPVGRVHRLLRRGNYAQRIGSGAPVYLTAV
LEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDDELN
KLLGNVTIAQGGVLPNIHQNLLP
D:  KETYSSYIYKVLKQTHPDTGISQKSMSILNSFVNDIFERI
ATEASKLAAYNKKSTISAREIQTAVRLILPGELAKHAVSE
GTRAVTKYSSSTQ
E:  KKPHRYKPGTVALREIRRFQKSTELLIRKLPFQRLVREIA
QDFKTDLRFQSSAIGALQESVEAYLVSLFEDTNLAAIHAK
RVTIQKKDIKLARRLRGE
F:  GGAKRHRKILRDNIQGITKPAIRRLARRGGVKRISGLIYE
EVRAVLKSFLESVIRDSVTYTEHAKRKTVTSLDVVYALKR
QGRTLYGFGG
G:  SQSRSAKAGLTFPVGRVHRLLRRGNYAQRIGSGAPVYLTA
VLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDDEL
NKLLGNVTIAQGGVLPNIHQNLLPK
H:  RKETYSSYIYKVLKQTHPDTGISQKSMSILNSFVNDIFER
IATEASKLAAYNKKSTISAREIQTAVRLILPGELAKHAVS
EGTRAVTKYSSSTQ
I:  ATCAATATCCACCTGCAGATTCTACCAAAAGTGTATTTGG
AAACTGCTCCATCAAAAGGCATGTTCAGCGGAATTCCGCT
GAACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTTT
GGTAGAATCTGCAGGTGGATATTGAT
J:  ATCAATATCCACCTGCAGATTCTACCAAAAGTGTATTTGG
AAACTGCTCCATCAAAAGGCATGTTCAGCGGAATTCCGCT
GAACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTTT
GGTAGAATCTGCAGGTGGATATTGAT
Description


Functional site

1) chain D
residue 123
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:10642555, ECO:0000269|PubMed:12535538, ECO:0000269|PubMed:12535539, ECO:0000269|PubMed:14660635, ECO:0000269|PubMed:15280549, ECO:0000269|PubMed:16432255
source Swiss-Prot : SWS_FT_FI11

2) chain H
residue 123
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:10642555, ECO:0000269|PubMed:12535538, ECO:0000269|PubMed:12535539, ECO:0000269|PubMed:14660635, ECO:0000269|PubMed:15280549, ECO:0000269|PubMed:16432255
source Swiss-Prot : SWS_FT_FI11

3) chain F
residue 31
type MOD_RES
sequence K
description N6-acetyllysine; alternate => ECO:0000269|PubMed:11545749, ECO:0000269|PubMed:15186774, ECO:0000269|PubMed:16598039, ECO:0000269|PubMed:19113941
source Swiss-Prot : SWS_FT_FI4

4) chain F
residue 77
type MOD_RES
sequence K
description N6-acetyllysine; alternate => ECO:0000269|PubMed:11545749, ECO:0000269|PubMed:15186774, ECO:0000269|PubMed:16598039, ECO:0000269|PubMed:19113941
source Swiss-Prot : SWS_FT_FI4

5) chain G
residue 21
type MOD_RES
sequence K
description N6-acetyllysine; alternate => ECO:0000269|PubMed:19113941
source Swiss-Prot : SWS_FT_FI5

6) chain D
residue 46
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000269|PubMed:22389435
source Swiss-Prot : SWS_FT_FI8

7) chain H
residue 46
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000269|PubMed:22389435
source Swiss-Prot : SWS_FT_FI8

8) chain D
residue 37
type MOD_RES
sequence K
description N6,N6-dimethyllysine => ECO:0000269|PubMed:19113941
source Swiss-Prot : SWS_FT_FI9

9) chain H
residue 37
type MOD_RES
sequence K
description N6,N6-dimethyllysine => ECO:0000269|PubMed:19113941
source Swiss-Prot : SWS_FT_FI9

10) chain D
residue 95-117
type prosite
sequence REIQTAVRLILPGELAKHAVSEG
description HISTONE_H2B Histone H2B signature. REIQTavRlILpGELaKHAVSEG
source prosite : PS00357

11) chain A
residue 66-74
type prosite
sequence PFQRLVREI
description HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI
source prosite : PS00959

12) chain C
residue 22-28
type prosite
sequence AGLTFPV
description HISTONE_H2A Histone H2A signature. AGLtFPV
source prosite : PS00046


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