7BMJ
Aspartyl/Asparaginyl beta-hydroxylase (AspH) oxygenase and TPR domains in complex with manganese, 5-fluoropyridine-2,4-dicarboxylic acid, and factor X substrate peptide fragment (39mer-4Ser)
Functional 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 |
C | 0018193 | biological_process | peptidyl-amino acid modification |
C | 0042264 | biological_process | peptidyl-aspartic acid hydroxylation |
C | 0062101 | molecular_function | peptidyl-aspartic acid 3-dioxygenase activity |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | MOD_RES: (3R)-3-hydroxyaspartate => ECO:0000269|PubMed:6871167 |
Chain | Residue | Details |
B | ASP103 | |
A | SER668 | |
A | ARG688 | |
A | ARG735 | |
C | TRP625 | |
C | SER668 | |
C | ARG688 | |
C | ARG735 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000305 |
Chain | Residue | Details |
A | HIS679 | |
A | HIS725 | |
C | HIS679 | |
C | HIS725 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine |
Chain | Residue | Details |
A | ASN452 | |
C | ASN452 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN706 | |
C | ASN706 |