6HA7
Crystal structure of the BiP NBD and MANF complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005524 | molecular_function | ATP binding |
| A | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| B | 0005524 | molecular_function | ATP binding |
| B | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| C | 0002014 | biological_process | vasoconstriction of artery involved in ischemic response to lowering of systemic arterial blood pressure |
| C | 0003674 | molecular_function | molecular_function |
| C | 0005575 | cellular_component | cellular_component |
| C | 0005576 | cellular_component | extracellular region |
| C | 0005615 | cellular_component | extracellular space |
| C | 0005783 | cellular_component | endoplasmic reticulum |
| C | 0005788 | cellular_component | endoplasmic reticulum lumen |
| C | 0006986 | biological_process | response to unfolded protein |
| C | 0007165 | biological_process | signal transduction |
| C | 0008083 | molecular_function | growth factor activity |
| C | 0008289 | molecular_function | lipid binding |
| C | 0016529 | cellular_component | sarcoplasmic reticulum |
| C | 0031175 | biological_process | neuron projection development |
| C | 0033018 | cellular_component | sarcoplasmic reticulum lumen |
| C | 0048471 | cellular_component | perinuclear region of cytoplasm |
| C | 0071542 | biological_process | dopaminergic neuron differentiation |
| C | 0120146 | molecular_function | sulfatide binding |
| C | 1905897 | biological_process | regulation of response to endoplasmic reticulum stress |
| D | 0002014 | biological_process | vasoconstriction of artery involved in ischemic response to lowering of systemic arterial blood pressure |
| D | 0003674 | molecular_function | molecular_function |
| D | 0005575 | cellular_component | cellular_component |
| D | 0005576 | cellular_component | extracellular region |
| D | 0005615 | cellular_component | extracellular space |
| D | 0005783 | cellular_component | endoplasmic reticulum |
| D | 0005788 | cellular_component | endoplasmic reticulum lumen |
| D | 0006986 | biological_process | response to unfolded protein |
| D | 0007165 | biological_process | signal transduction |
| D | 0008083 | molecular_function | growth factor activity |
| D | 0008289 | molecular_function | lipid binding |
| D | 0016529 | cellular_component | sarcoplasmic reticulum |
| D | 0031175 | biological_process | neuron projection development |
| D | 0033018 | cellular_component | sarcoplasmic reticulum lumen |
| D | 0048471 | cellular_component | perinuclear region of cytoplasm |
| D | 0071542 | biological_process | dopaminergic neuron differentiation |
| D | 0120146 | molecular_function | sulfatide binding |
| D | 1905897 | biological_process | regulation of response to endoplasmic reticulum stress |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 501 |
| Chain | Residue |
| A | ASP34 |
| A | GLY36 |
| A | VAL394 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 501 |
| Chain | Residue |
| B | ASP34 |
| B | GLY36 |
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. VFDLGGGTfdvSLL |
| 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 | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18034455 |
| Chain | Residue | Details |
| C | TYR73 | |
| D | TYR73 | |
| A | GLU293 | |
| A | GLY364 | |
| B | GLY36 | |
| B | GLY227 | |
| B | GLU293 | |
| B | GLY364 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P11021 |
| Chain | Residue | Details |
| A | LYS96 | |
| B | LYS96 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P06761 |
| Chain | Residue | Details |
| A | SER86 | |
| B | SER86 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P20029 |
| Chain | Residue | Details |
| A | LYS125 | |
| A | LYS213 | |
| A | LYS326 | |
| B | LYS125 | |
| B | LYS213 | |
| B | LYS326 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: 3'-nitrotyrosine => ECO:0000250|UniProtKB:P20029 |
| Chain | Residue | Details |
| A | TYR160 | |
| B | TYR160 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P0DMV8 |
| Chain | Residue | Details |
| A | LYS271 | |
| B | LYS271 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P20029 |
| Chain | Residue | Details |
| A | LYS353 | |
| B | LYS353 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000250|UniProtKB:P11021 |
| Chain | Residue | Details |
| A | LYS352 | |
| B | LYS352 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate => ECO:0000250|UniProtKB:P11021 |
| Chain | Residue | Details |
| A | LYS353 | |
| B | LYS353 |
