1HQ3
CRYSTAL STRUCTURE OF THE HISTONE-CORE-OCTAMER IN KCL/PHOSPHATE
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000786 | cellular_component | nucleosome |
A | 0003677 | molecular_function | DNA binding |
A | 0005634 | cellular_component | nucleus |
A | 0005694 | cellular_component | chromosome |
A | 0030527 | molecular_function | structural constituent of chromatin |
A | 0031492 | molecular_function | nucleosomal DNA binding |
A | 0046982 | molecular_function | protein heterodimerization activity |
A | 0070828 | biological_process | heterochromatin organization |
B | 0000786 | cellular_component | nucleosome |
B | 0003677 | molecular_function | DNA binding |
B | 0005634 | cellular_component | nucleus |
B | 0005694 | cellular_component | chromosome |
B | 0030527 | molecular_function | structural constituent of chromatin |
B | 0044877 | molecular_function | protein-containing complex binding |
B | 0046982 | molecular_function | protein heterodimerization activity |
C | 0000122 | biological_process | negative regulation of transcription by RNA polymerase II |
C | 0000785 | cellular_component | chromatin |
C | 0000786 | cellular_component | nucleosome |
C | 0003677 | molecular_function | DNA binding |
C | 0003682 | molecular_function | chromatin binding |
C | 0005634 | cellular_component | nucleus |
C | 0005694 | cellular_component | chromosome |
C | 0010467 | biological_process | gene expression |
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 | 0005634 | cellular_component | nucleus |
D | 0005654 | cellular_component | nucleoplasm |
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 |
E | 0000786 | cellular_component | nucleosome |
E | 0003677 | molecular_function | DNA binding |
E | 0005634 | cellular_component | nucleus |
E | 0005694 | cellular_component | chromosome |
E | 0030527 | molecular_function | structural constituent of chromatin |
E | 0031492 | molecular_function | nucleosomal DNA binding |
E | 0046982 | molecular_function | protein heterodimerization activity |
E | 0070828 | biological_process | heterochromatin organization |
F | 0000786 | cellular_component | nucleosome |
F | 0003677 | molecular_function | DNA binding |
F | 0005634 | cellular_component | nucleus |
F | 0005694 | cellular_component | chromosome |
F | 0030527 | molecular_function | structural constituent of chromatin |
F | 0044877 | molecular_function | protein-containing complex binding |
F | 0046982 | molecular_function | protein heterodimerization activity |
G | 0000122 | biological_process | negative regulation of transcription by RNA polymerase II |
G | 0000785 | cellular_component | chromatin |
G | 0000786 | cellular_component | nucleosome |
G | 0003677 | molecular_function | DNA binding |
G | 0003682 | molecular_function | chromatin binding |
G | 0005634 | cellular_component | nucleus |
G | 0005694 | cellular_component | chromosome |
G | 0010467 | biological_process | gene expression |
G | 0030527 | molecular_function | structural constituent of chromatin |
G | 0046982 | molecular_function | protein heterodimerization activity |
H | 0000786 | cellular_component | nucleosome |
H | 0003677 | molecular_function | DNA binding |
H | 0005634 | cellular_component | nucleus |
H | 0005654 | cellular_component | nucleoplasm |
H | 0005694 | cellular_component | chromosome |
H | 0006334 | biological_process | nucleosome assembly |
H | 0030527 | molecular_function | structural constituent of chromatin |
H | 0046982 | molecular_function | protein heterodimerization activity |
Functional Information from PDB Data
site_id | 1 |
Number of Residues | |
Details |
Chain | Residue |
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 A 501 |
Chain | Residue |
A | ARG29 |
A | ARG32 |
A | LYS36 |
A | HOH661 |
D | LYS31 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 B 502 |
Chain | Residue |
A | ARG77 |
B | SER55 |
B | SER56 |
B | HOH657 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PO4 E 503 |
Chain | Residue |
E | ARG29 |
E | ARG32 |
E | LYS36 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 E 504 |
Chain | Residue |
E | ARG77 |
E | HOH653 |
F | SER55 |
F | SER56 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 C 505 |
Chain | Residue |
C | GLU50 |
C | ARG53 |
C | TYR54 |
D | ARG36 |
D | HOH660 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL G 601 |
Chain | Residue |
G | LEU60 |
G | LYS64 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL E 602 |
Chain | Residue |
E | GLY46 |
E | ALA47 |
F | THR90 |
F | SER91 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL D 603 |
Chain | Residue |
D | ARG39 |
D | ILE46 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL A 604 |
Chain | Residue |
A | ARG35 |
D | LYS31 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL H 605 |
Chain | Residue |
A | THR101 |
A | HOH666 |
H | ARG95 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL A 606 |
Chain | Residue |
A | GLY44 |
A | GLY46 |
A | ALA47 |
B | THR90 |
B | SER91 |
site_id | BC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL C 607 |
Chain | Residue |
C | LYS122 |
site_id | BC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL G 608 |
Chain | Residue |
G | PRO121 |
G | LYS122 |
site_id | BC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL G 609 |
Chain | Residue |
G | ARG116 |
G | VAL117 |
G | THR118 |
site_id | BC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL H 610 |
Chain | Residue |
H | ARG35 |
H | ARG39 |
H | ILE46 |
site_id | BC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL G 611 |
Chain | Residue |
G | GLN68 |
G | ARG69 |
G | ARG72 |
site_id | BC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL D 612 |
Chain | Residue |
C | ARG63 |
D | GLY28 |
D | THR30 |
D | ALA33 |
site_id | BC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL A 613 |
Chain | Residue |
A | LEU85 |
A | ASN89 |
site_id | CC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL B 614 |
Chain | Residue |
B | LYS34 |
B | SER64 |
B | HOH632 |
H | GLY101 |
H | HOH620 |
site_id | CC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL C 615 |
Chain | Residue |
C | ARG116 |
C | VAL117 |
C | THR118 |
site_id | CC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL F 616 |
Chain | Residue |
F | LYS116 |
H | LEU22 |
H | ARG23 |
H | ASN25 |
site_id | CC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL D 617 |
Chain | Residue |
C | ALA95 |
D | ARG95 |
E | THR101 |
site_id | CC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL H 618 |
Chain | Residue |
F | LYS108 |
H | THR30 |
H | LYS31 |
site_id | CC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL C 619 |
Chain | Residue |
C | GLN125 |
C | ARG128 |
C | ARG134 |
site_id | CC7 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL A 620 |
Chain | Residue |
A | ILE111 |
site_id | CC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL E 621 |
Chain | Residue |
E | ARG17 |
E | SER18 |
E | GLY28 |
site_id | CC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL A 622 |
Chain | Residue |
A | ARG29 |
D | LYS31 |
Functional Information from PROSITE/UniProt
site_id | PS00047 |
Number of Residues | 5 |
Details | HISTONE_H4 Histone H4 signature. GAKRH |
Chain | Residue | Details |
D | GLY14-HIS18 |
site_id | PS00046 |
Number of Residues | 7 |
Details | HISTONE_H2A Histone H2A signature. AGLqFPV |
Chain | Residue | Details |
A | ALA21-VAL27 |
site_id | PS00322 |
Number of Residues | 7 |
Details | HISTONE_H3_1 Histone H3 signature 1. KAPRKQL |
Chain | Residue | Details |
C | LYS14-LEU20 |
site_id | PS00959 |
Number of Residues | 9 |
Details | HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI |
Chain | Residue | Details |
C | PRO66-ILE74 |
site_id | PS00357 |
Number of Residues | 23 |
Details | HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG |
Chain | Residue | Details |
B | ARG92-GLY114 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | DNA_BIND: |
Chain | Residue | Details |
D | LYS16-LYS20 | |
H | LYS16-LYS20 | |
B | LYS15 | |
B | LYS20 | |
F | LYS5 | |
F | LYS12 | |
F | LYS15 | |
F | LYS20 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P62805 |
Chain | Residue | Details |
D | SER1 | |
H | SER1 | |
G | ARG2 | |
G | ARG17 |
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 |
D | ARG3 | |
H | ARG3 | |
E | LYS9 | |
E | LYS95 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N6-lactoyllysine; alternate => ECO:0000250|UniProtKB:P62805 |
Chain | Residue | Details |
D | LYS5 | |
H | LYS5 | |
F | LYS120 |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | MOD_RES: N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805 |
Chain | Residue | Details |
D | LYS8 | |
D | LYS16 | |
D | LYS44 | |
D | LYS79 | |
H | LYS8 | |
H | LYS16 | |
H | LYS44 | |
H | LYS79 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:P62805 |
Chain | Residue | Details |
D | LYS12 | |
D | LYS20 | |
H | LYS12 | |
H | LYS20 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62805 |
Chain | Residue | Details |
D | LYS31 | |
D | LYS91 | |
H | LYS31 | |
H | LYS91 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; by PAK2 => ECO:0000250|UniProtKB:P62805 |
Chain | Residue | Details |
D | SER47 | |
H | SER47 | |
E | LYS118 | |
E | LYS119 |
site_id | SWS_FT_FI9 |
Number of Residues | 4 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P62805 |
Chain | Residue | Details |
D | TYR51 | |
D | TYR88 | |
H | TYR51 | |
H | TYR88 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | MOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 |
Chain | Residue | Details |
D | LYS59 | |
H | LYS59 | |
E | LYS119 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P62805 |
Chain | Residue | Details |
D | LYS77 | |
H | LYS77 | |
C | LYS64 | |
G | LYS18 | |
G | LYS23 | |
G | LYS64 |
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 |
D | LYS31 | |
H | LYS31 |
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 | LYS27 | |
D | LYS91 | |
G | LYS27 | |
H | LYS91 |
site_id | SWS_FT_FI14 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5 => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
C | SER28 | |
G | SER28 |
site_id | SWS_FT_FI15 |
Number of Residues | 2 |
Details | MOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68431 |
Chain | Residue | Details |
C | LYS37 | |
G | LYS37 |
site_id | SWS_FT_FI16 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
C | TYR41 | |
G | TYR41 |
site_id | SWS_FT_FI17 |
Number of Residues | 4 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 |
Chain | Residue | Details |
C | LYS56 | |
C | LYS79 | |
G | LYS56 | |
G | LYS79 |
site_id | SWS_FT_FI18 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
C | SER57 | |
G | SER57 |
site_id | SWS_FT_FI19 |
Number of Residues | 4 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
C | THR80 | |
C | THR107 | |
G | THR80 | |
G | THR107 |
site_id | SWS_FT_FI20 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P84243 |
Chain | Residue | Details |
C | SER86 | |
G | SER86 |
site_id | SWS_FT_FI21 |
Number of Residues | 2 |
Details | MOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
C | LYS115 | |
G | LYS115 |
site_id | SWS_FT_FI22 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
C | LYS122 | |
G | LYS122 |
site_id | SWS_FT_FI23 |
Number of Residues | 2 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
C | CYS110 | |
G | CYS110 |