6RK9
Aspartyl/Asparaginyl beta-hydroxylase (AspH)oxygenase and TPR domains in complex with manganese, N-oxalylglycine and cyclic peptide substrate mimic of factor X
Replaces: 5JZZFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0018193 | biological_process | peptidyl-amino acid modification |
| A | 0042264 | biological_process | peptidyl-aspartic acid hydroxylation |
| A | 0062101 | molecular_function | peptidyl-aspartic acid 3-dioxygenase activity |
| B | 0018193 | biological_process | peptidyl-amino acid modification |
| B | 0042264 | biological_process | peptidyl-aspartic acid hydroxylation |
| B | 0062101 | molecular_function | peptidyl-aspartic acid 3-dioxygenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue MN A 801 |
| Chain | Residue |
| A | HIS679 |
| A | HIS725 |
| A | OGA802 |
| C | ASP255 |
| C | HOH301 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue OGA A 802 |
| Chain | Residue |
| A | ARG688 |
| A | HIS690 |
| A | HIS725 |
| A | ARG735 |
| A | ILE737 |
| A | ILE739 |
| A | MN801 |
| C | ASP255 |
| A | TRP625 |
| A | SER668 |
| A | MET670 |
| A | HIS679 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue MN B 801 |
| Chain | Residue |
| B | HIS679 |
| B | HIS725 |
| B | OGA802 |
| B | HOH925 |
| B | HOH957 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | binding site for residue OGA B 802 |
| Chain | Residue |
| B | TRP625 |
| B | SER668 |
| B | MET670 |
| B | HIS679 |
| B | ARG688 |
| B | HIS690 |
| B | PHE719 |
| B | HIS725 |
| B | ARG735 |
| B | ILE737 |
| B | MN801 |
| B | HOH957 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | binding site for Di-peptide DAL C 253 and LYS C 254 |
| Chain | Residue |
| A | GLU617 |
| A | GLN664 |
| A | PRO682 |
| A | ARG686 |
| A | ILE758 |
| A | HOH915 |
| C | ASP255 |
| C | GLY256 |
| C | GLU259 |
| C | CYS262 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 66 |
| Details | Repeat: {"description":"TPR 1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 66 |
| Details | Repeat: {"description":"TPR 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 64 |
| Details | Repeat: {"description":"TPR 3"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 64 |
| Details | Repeat: {"description":"TPR 4"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2011","submissionDatabase":"PDB data bank","title":"Crystal structure of human aspartate beta-hydroxylase isoform A.","authoringGroup":["Structural genomics consortium (SGC)"]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
