6Q9F
Aspartyl/Asparaginyl beta-hydroxylase (AspH) H679A in complex with Mn, NOG and Factor X peptide fragment (39mer-4Ser)
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue MN A 901 |
| Chain | Residue |
| A | HIS725 |
| A | OGA902 |
| A | HOH1065 |
| A | HOH1198 |
| A | HOH1259 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | binding site for residue OGA A 902 |
| Chain | Residue |
| A | HIS690 |
| A | PHE719 |
| A | ASP721 |
| A | HIS725 |
| A | VAL727 |
| A | ARG735 |
| A | ILE737 |
| A | ILE739 |
| A | MN901 |
| A | HOH1065 |
| A | HOH1198 |
| A | HOH1208 |
| A | TRP625 |
| A | SER668 |
| A | MET670 |
| A | ARG688 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 903 |
| Chain | Residue |
| A | LYS595 |
| A | LYS609 |
| A | SER626 |
| A | HIS671 |
| A | HOH1005 |
| A | HOH1007 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 904 |
| Chain | Residue |
| A | SER455 |
| A | ASN458 |
| A | ASP459 |
| A | PHE489 |
| A | HOH1107 |
| A | HOH1137 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 905 |
| Chain | Residue |
| A | ALA500 |
| A | ASP616 |
| A | ASN618 |
| A | HOH1015 |
| A | HOH1042 |
| A | HOH1342 |
| B | GLY106 |
| B | GLU107 |
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 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"(3R)-3-hydroxyaspartate","evidences":[{"source":"PubMed","id":"6871167","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
