5JZA
Aspartyl/Asparaginyl beta-hydroxylase (AspH)oxygenase and TPR domains in complex with manganese and N-oxalylglycine
Functional Information from GO Data
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 | OGA806 |
| A | HOH939 |
| A | HOH1005 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 802 |
| Chain | Residue |
| A | HOH931 |
| A | SER455 |
| A | ASN458 |
| A | ASP459 |
| A | PRO520 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 803 |
| Chain | Residue |
| A | TYR544 |
| A | TRP560 |
| A | GOL804 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 804 |
| Chain | Residue |
| A | TRP560 |
| A | ASN706 |
| A | GOL803 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue GOL A 805 |
| Chain | Residue |
| A | LEU466 |
| A | ARG526 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | binding site for residue OGA A 806 |
| Chain | Residue |
| A | TRP625 |
| A | SER668 |
| A | MET670 |
| A | HIS679 |
| A | ARG688 |
| A | HIS690 |
| A | HIS725 |
| A | VAL727 |
| A | ARG735 |
| A | ILE739 |
| A | MN801 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 33 |
| Details | Repeat: {"description":"TPR 1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 33 |
| Details | Repeat: {"description":"TPR 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 32 |
| Details | Repeat: {"description":"TPR 3"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 32 |
| Details | Repeat: {"description":"TPR 4"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 5 |
| 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 | 2 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
