4F9Z
Crystal Structure of human ERp27
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003756 | molecular_function | protein disulfide isomerase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005788 | cellular_component | endoplasmic reticulum lumen |
| A | 0006457 | biological_process | protein folding |
| A | 0006986 | biological_process | response to unfolded protein |
| A | 0034976 | biological_process | response to endoplasmic reticulum stress |
| B | 0003756 | molecular_function | protein disulfide isomerase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0005788 | cellular_component | endoplasmic reticulum lumen |
| B | 0006457 | biological_process | protein folding |
| B | 0006986 | biological_process | response to unfolded protein |
| B | 0034976 | biological_process | response to endoplasmic reticulum stress |
| C | 0003756 | molecular_function | protein disulfide isomerase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005783 | cellular_component | endoplasmic reticulum |
| C | 0005788 | cellular_component | endoplasmic reticulum lumen |
| C | 0006457 | biological_process | protein folding |
| C | 0006986 | biological_process | response to unfolded protein |
| C | 0034976 | biological_process | response to endoplasmic reticulum stress |
| D | 0003756 | molecular_function | protein disulfide isomerase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005783 | cellular_component | endoplasmic reticulum |
| D | 0005788 | cellular_component | endoplasmic reticulum lumen |
| D | 0006457 | biological_process | protein folding |
| D | 0006986 | biological_process | response to unfolded protein |
| D | 0034976 | biological_process | response to endoplasmic reticulum stress |
| E | 0003756 | molecular_function | protein disulfide isomerase activity |
| E | 0005515 | molecular_function | protein binding |
| E | 0005783 | cellular_component | endoplasmic reticulum |
| E | 0005788 | cellular_component | endoplasmic reticulum lumen |
| E | 0006457 | biological_process | protein folding |
| E | 0006986 | biological_process | response to unfolded protein |
| E | 0034976 | biological_process | response to endoplasmic reticulum stress |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT D 301 |
| Chain | Residue |
| D | HIS180 |
| D | HOH447 |
| E | PHE212 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT D 302 |
| Chain | Residue |
| B | ALA54 |
| D | GLU137 |
| D | ASN148 |
| D | HOH436 |
| D | HOH441 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT D 303 |
| Chain | Residue |
| D | PHE189 |
| D | GLN246 |
| D | ASP250 |
| D | LEU188 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT D 304 |
| Chain | Residue |
| A | ASP92 |
| D | HIS98 |
| D | ASN100 |
| E | ALA129 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT A 302 |
| Chain | Residue |
| A | LEU188 |
| A | GLN246 |
| A | ASP250 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT A 303 |
| Chain | Residue |
| A | LEU188 |
| B | PHE156 |
| B | SER158 |
| B | GLN161 |
| B | THR227 |
| site_id | AC7 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PE3 B 301 |
| Chain | Residue |
| B | HIS180 |
| B | GLN183 |
| B | LYS184 |
| B | LYS187 |
| D | TYR147 |
| D | PHE211 |
| D | TYR225 |
| D | GLN226 |
| D | ASP229 |
| D | ASP230 |
| D | GLU231 |
| D | TRP232 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT B 302 |
| Chain | Residue |
| B | LEU188 |
| B | PHE189 |
| B | GLN246 |
| B | ASP250 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACT B 303 |
| Chain | Residue |
| B | ASP233 |
| B | HOH501 |
| site_id | BC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PE4 C 301 |
| Chain | Residue |
| A | TYR147 |
| A | ASN148 |
| A | PRO149 |
| A | ASN205 |
| A | VAL208 |
| C | HIS180 |
| C | GLN183 |
| C | LYS184 |
| C | LYS187 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT C 302 |
| Chain | Residue |
| C | TYR147 |
| C | TYR225 |
| C | HOH419 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT C 303 |
| Chain | Residue |
| C | ASN157 |
| C | SER158 |
| C | GLN161 |
| C | HOH505 |
| E | GLN246 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT E 301 |
| Chain | Residue |
| A | ASP233 |
| A | THR234 |
| E | GLU231 |
| E | SER254 |
| E | LYS256 |
| E | HOH498 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT E 302 |
| Chain | Residue |
| C | LEU228 |
| E | GLU243 |
| E | GLN246 |
| E | HOH467 |
| E | HOH540 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 5 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 |
| Chain | Residue | Details |
| D | ASN100 | |
| A | ASN100 | |
| B | ASN100 | |
| C | ASN100 | |
| E | ASN100 |
