6ZMD
Crystal structure of HYPE covalently tethered to BiP bound to AMP-PNP
Functional Information from GO Data
Functional Information from PROSITE/UniProt
site_id | PS00297 |
Number of Residues | 8 |
Details | HSP70_1 Heat shock hsp70 proteins family signature 1. IDLGTTyS |
Chain | Residue | Details |
A | ILE33-SER40 |
site_id | PS00329 |
Number of Residues | 14 |
Details | HSP70_2 Heat shock hsp70 proteins family signature 2. VFDLGGGAfdvSLL |
Chain | Residue | Details |
A | VAL222-LEU235 |
site_id | PS01036 |
Number of Residues | 15 |
Details | HSP70_3 Heat shock hsp70 proteins family signature 3. IvLvGGsTRIPkIqQ |
Chain | Residue | Details |
A | ILE359-GLN373 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:22266942 |
Chain | Residue | Details |
B | HIS363 | |
A | LYS96 | |
A | GLY227 | |
A | GLU293 | |
A | GLY364 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:25435325, ECO:0007744|PDB:4U07, ECO:0007744|PDB:4U0U |
Chain | Residue | Details |
B | GLY234 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:25435325, ECO:0007744|PDB:4U07, ECO:0007744|PDB:4U0S, ECO:0007744|PDB:4U0U |
Chain | Residue | Details |
B | VAL316 | |
B | TYR399 | |
B | ASN407 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:25435325, ECO:0007744|PDB:4U07 |
Chain | Residue | Details |
B | ASP367 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | SITE: Important for autoinhibition of adenylyltransferase activity => ECO:0000269|PubMed:22266942, ECO:0000269|PubMed:25435325 |
Chain | Residue | Details |
B | GLY234 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: O-AMP-threonine; by autocatalysis => ECO:0000305|PubMed:25601083 |
Chain | Residue | Details |
B | ALA183 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:25601083 |
Chain | Residue | Details |
B | ASN275 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:P0DMV8 |
Chain | Residue | Details |
A | ARG492 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; alternate => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | THR518 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25114211, ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733 |
Chain | Residue | Details |
A | LYS352 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate => ECO:0007744|PubMed:25114211 |
Chain | Residue | Details |
A | LYS353 |