eF-site ID 4qr9-B PDB Code 4qr9 Chain B click to enlarge Title Crystal structure of two HMGB1 Box A domains cooperating to underwind and kink a DNA Classification DNA BINDING PROTEIN Compound High mobility group protein B1 Source Rattus norvegicus (Rat) (4QR9) Sequence B:  GSKPRGKMSSYAFFVQTCREEHKKKHPDASVNFSEFSKKC SERWKTMSAKEKGKFEDMAKADKARYEREMKTYIP Description Functional site 1) chain B residue 67 type CROSSLNK sequence K description Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-?) => ECO:0000250|UniProtKB:P09429 source Swiss-Prot : SWS_FT_FI8 2) chain B residue 27 type CROSSLNK sequence K description Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-?) => ECO:0000250|UniProtKB:P09429 source Swiss-Prot : SWS_FT_FI8 3) chain B residue 42 type CROSSLNK sequence K description Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-?) => ECO:0000250|UniProtKB:P09429 source Swiss-Prot : SWS_FT_FI8 4) chain B residue 43 type CROSSLNK sequence K description Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-?) => ECO:0000250|UniProtKB:P09429 source Swiss-Prot : SWS_FT_FI8 5) chain B residue 8-78 type DNA_BIND sequence PRGKMSSYAFFVQTCREEHKKKHPDASVNFSEFSKKCSER WKTMSAKEKGKFEDMAKADKARYEREMKTYI description HMG box 1 => ECO:0000255|PROSITE-ProRule:PRU00267 source Swiss-Prot : SWS_FT_FI1 6) chain B residue 9 type SITE sequence R description Cleavage; by thrombin:thrombomodulin => ECO:0000250|UniProtKB:P10103 source Swiss-Prot : SWS_FT_FI2 7) chain B residue 66 type SITE sequence D description Cleavage; by CASP1 => ECO:0000250|UniProtKB:P09429 source Swiss-Prot : SWS_FT_FI3 8) chain B residue 29 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P10103 source Swiss-Prot : SWS_FT_FI4 9) chain B residue 7 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P10103 source Swiss-Prot : SWS_FT_FI4 10) chain B residue 11 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P10103 source Swiss-Prot : SWS_FT_FI4 11) chain B residue 27 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P10103 source Swiss-Prot : SWS_FT_FI4 12) chain B residue 28 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P10103 source Swiss-Prot : SWS_FT_FI4 13) chain B residue 22 type MOD_RES sequence C description Cysteine sulfonic acid (-SO3H); alternate => ECO:0000305|PubMed:22869893 source Swiss-Prot : SWS_FT_FI5 14) chain B residue 44 type MOD_RES sequence C description Cysteine sulfonic acid (-SO3H); alternate => ECO:0000305|PubMed:22869893 source Swiss-Prot : SWS_FT_FI5 15) chain B residue 34 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P09429 source Swiss-Prot : SWS_FT_FI6 16) chain B residue 42 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P63158 source Swiss-Prot : SWS_FT_FI7

Display surface Download Links