2BKY
Crystal structure of the Alba1:Alba2 heterodimer from sulfolobus solfataricus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003690 | molecular_function | double-stranded DNA binding |
| A | 0003723 | molecular_function | RNA binding |
| A | 0004518 | molecular_function | nuclease activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005694 | cellular_component | chromosome |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0030261 | biological_process | chromosome condensation |
| A | 0042802 | molecular_function | identical protein binding |
| B | 0003676 | molecular_function | nucleic acid binding |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003690 | molecular_function | double-stranded DNA binding |
| B | 0003723 | molecular_function | RNA binding |
| B | 0004518 | molecular_function | nuclease activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005694 | cellular_component | chromosome |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0030261 | biological_process | chromosome condensation |
| B | 0042802 | molecular_function | identical protein binding |
| X | 0003676 | molecular_function | nucleic acid binding |
| X | 0003677 | molecular_function | DNA binding |
| X | 0003690 | molecular_function | double-stranded DNA binding |
| X | 0003723 | molecular_function | RNA binding |
| X | 0005515 | molecular_function | protein binding |
| X | 0005694 | cellular_component | chromosome |
| X | 0005737 | cellular_component | cytoplasm |
| X | 0030261 | biological_process | chromosome condensation |
| Y | 0003676 | molecular_function | nucleic acid binding |
| Y | 0003677 | molecular_function | DNA binding |
| Y | 0003690 | molecular_function | double-stranded DNA binding |
| Y | 0003723 | molecular_function | RNA binding |
| Y | 0005515 | molecular_function | protein binding |
| Y | 0005694 | cellular_component | chromosome |
| Y | 0005737 | cellular_component | cytoplasm |
| Y | 0030261 | biological_process | chromosome condensation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MPD A 1098 |
| Chain | Residue |
| A | THR78 |
| A | SER79 |
| A | GLY82 |
| A | HOH2033 |
| Y | ASN65 |
| Y | VAL66 |
| Y | GLN67 |
| Y | MPD1090 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD A 1099 |
| Chain | Residue |
| A | HOH2088 |
| X | ARG41 |
| X | HOH2041 |
| A | ASP51 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MPD B 1098 |
| Chain | Residue |
| B | THR78 |
| B | SER79 |
| B | HOH2092 |
| B | HOH2093 |
| X | ASN65 |
| X | VAL66 |
| X | GLN67 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MPD X 1090 |
| Chain | Residue |
| Y | ARG75 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MPD Y 1090 |
| Chain | Residue |
| A | GLN80 |
| A | MPD1098 |
| B | ILE67 |
| B | ILE70 |
| Y | ASN65 |
| Y | VAL66 |
| Y | GLN67 |
| Y | HOH2062 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12837780, ECO:0007744|PDB:1UDV |
| Chain | Residue | Details |
| X | LYS14 | |
| B | ARG44 | |
| X | ASP18 | |
| X | ASP22 | |
| Y | LYS14 | |
| Y | ASP18 | |
| Y | ASP22 | |
| B | LYS17 | |
| B | TYR22 | |
| B | ARG42 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000255|HAMAP-Rule:MF_01122 |
| Chain | Residue | Details |
| X | LYS12 | |
| Y | LYS12 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylserine; by ard1 acetylase => ECO:0000269|PubMed:11935028, ECO:0000269|PubMed:17511810, ECO:0000269|PubMed:29679495 |
| Chain | Residue | Details |
| A | SER2 | |
| B | SER2 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:29679495 |
| Chain | Residue | Details |
| A | LYS16 | |
| B | LYS16 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: Deamidated asparagine; partial => ECO:0000269|PubMed:29679495 |
| Chain | Residue | Details |
| A | ASN31 | |
| A | ASN58 | |
| B | ASN31 | |
| B | ASN58 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Deamidated glutamine; partial => ECO:0000269|PubMed:29679495 |
| Chain | Residue | Details |
| A | GLN32 | |
| B | GLN32 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-methyllysine; partial => ECO:0000269|PubMed:29679495 |
| Chain | Residue | Details |
| A | LYS40 | |
| A | LYS97 | |
| B | LYS40 | |
| B | LYS97 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine; partial => ECO:0000269|PubMed:29679495 |
| Chain | Residue | Details |
| A | LYS48 | |
| A | LYS68 | |
| B | LYS48 | |
| B | LYS68 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | MOD_RES: Aspartate methyl ester; partial => ECO:0000269|PubMed:29679495 |
| Chain | Residue | Details |
| A | ASP51 | |
| A | ASP81 | |
| B | ASP51 | |
| B | ASP81 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-methyllysine; alternate; partial => ECO:0000269|PubMed:29679495 |
| Chain | Residue | Details |
| A | LYS64 | |
| B | LYS64 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | MOD_RES: Glutamate methyl ester (Glu); partial => ECO:0000269|PubMed:29679495 |
| Chain | Residue | Details |
| A | GLU69 | |
| B | GLU69 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | MOD_RES: N5-methylglutamine; partial => ECO:0000269|PubMed:29679495 |
| Chain | Residue | Details |
| A | GLN75 | |
| B | GLN75 |
