2E9E
Crystal structure of the complex of goat lactoperoxidase with Nitrate at 3.25 A resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004601 | molecular_function | peroxidase activity |
| A | 0006979 | biological_process | response to oxidative stress |
| A | 0020037 | molecular_function | heme binding |
| B | 0004601 | molecular_function | peroxidase activity |
| B | 0006979 | biological_process | response to oxidative stress |
| B | 0020037 | molecular_function | heme binding |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00298 |
| Chain | Residue | Details |
| A | HIS109 | |
| B | HIS109 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: covalent => ECO:0000269|PubMed:18191143, ECO:0000269|PubMed:27398304, ECO:0000269|Ref.11, ECO:0000269|Ref.5, ECO:0000269|Ref.6, ECO:0000269|Ref.7, ECO:0007744|PDB:2E9E, ECO:0007744|PDB:2EFB, ECO:0007744|PDB:2EHA, ECO:0007744|PDB:2OJV, ECO:0007744|PDB:2R5L, ECO:0007744|PDB:3N8F, ECO:0007744|PDB:3NAK, ECO:0007744|PDB:3NIU, ECO:0007744|PDB:3QF1, ECO:0007744|PDB:3R55, ECO:0007744|PDB:3RKE, ECO:0007744|PDB:3SXV, ECO:0007744|PDB:4MSF, ECO:0007744|PDB:4OEK, ECO:0007744|PDB:4QJQ, ECO:0007744|PDB:5FF1, ECO:0007744|PDB:5HPW, ECO:0007744|PDB:6LF7, ECO:0007744|PDB:8ING |
| Chain | Residue | Details |
| A | ASP108 | |
| A | GLU258 | |
| B | ASP108 | |
| B | GLU258 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18191143, ECO:0000269|PubMed:27398304, ECO:0000269|Ref.11, ECO:0000269|Ref.5, ECO:0000269|Ref.6, ECO:0000269|Ref.7, ECO:0007744|PDB:2E9E, ECO:0007744|PDB:2EFB, ECO:0007744|PDB:2EHA, ECO:0007744|PDB:2OJV, ECO:0007744|PDB:2R5L, ECO:0007744|PDB:3N8F, ECO:0007744|PDB:3NAK, ECO:0007744|PDB:3NIU, ECO:0007744|PDB:3QF1, ECO:0007744|PDB:3R55, ECO:0007744|PDB:3RKE, ECO:0007744|PDB:3SXV, ECO:0007744|PDB:4MSF, ECO:0007744|PDB:4OEK, ECO:0007744|PDB:4QJQ, ECO:0007744|PDB:5FF1, ECO:0007744|PDB:5HPW, ECO:0007744|PDB:6LF7, ECO:0007744|PDB:8ING |
| Chain | Residue | Details |
| A | ASP110 | |
| B | SER190 | |
| A | THR184 | |
| A | PHE186 | |
| A | ASP188 | |
| A | SER190 | |
| B | ASP110 | |
| B | THR184 | |
| B | PHE186 | |
| B | ASP188 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: axial binding residue => ECO:0000269|PubMed:18191143, ECO:0000269|PubMed:27398304, ECO:0000269|Ref.11, ECO:0000269|Ref.5, ECO:0000269|Ref.6, ECO:0000269|Ref.7, ECO:0007744|PDB:2E9E, ECO:0007744|PDB:2EFB, ECO:0007744|PDB:2EHA, ECO:0007744|PDB:2OJV, ECO:0007744|PDB:2R5L, ECO:0007744|PDB:3N8F, ECO:0007744|PDB:3NAK, ECO:0007744|PDB:3NIU, ECO:0007744|PDB:3QF1, ECO:0007744|PDB:3R55, ECO:0007744|PDB:3RKE, ECO:0007744|PDB:3SXV, ECO:0007744|PDB:4MSF, ECO:0007744|PDB:4OEK, ECO:0007744|PDB:4QJQ, ECO:0007744|PDB:5FF1, ECO:0007744|PDB:5HPW, ECO:0007744|PDB:6LF7, ECO:0007744|PDB:8ING |
| Chain | Residue | Details |
| A | HIS351 | |
| B | HIS351 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | SITE: Transition state stabilizer => ECO:0000255|PROSITE-ProRule:PRU00298 |
| Chain | Residue | Details |
| A | ARG255 | |
| B | ARG255 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:18191143 |
| Chain | Residue | Details |
| A | SER198 | |
| B | SER198 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: 3'-nitrotyrosine => ECO:0000250|UniProtKB:P11678 |
| Chain | Residue | Details |
| A | TYR365 | |
| B | TYR365 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) (hybrid) asparagine; alternate => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:18191143, ECO:0000269|PubMed:27398304, ECO:0000269|PubMed:30296068, ECO:0000269|Ref.11, ECO:0000269|Ref.5, ECO:0000269|Ref.6, ECO:0000269|Ref.7, ECO:0007744|PDB:2E9E, ECO:0007744|PDB:2EFB, ECO:0007744|PDB:2EHA, ECO:0007744|PDB:2OJV, ECO:0007744|PDB:2R5L, ECO:0007744|PDB:3N8F, ECO:0007744|PDB:3NAK, ECO:0007744|PDB:3NIU, ECO:0007744|PDB:3R55, ECO:0007744|PDB:3RKE, ECO:0007744|PDB:3SXV, ECO:0007744|PDB:4MSF, ECO:0007744|PDB:4OEK, ECO:0007744|PDB:4QJQ, ECO:0007744|PDB:5FF1, ECO:0007744|PDB:5HPW, ECO:0007744|PDB:6LF7, ECO:0007744|PDB:8ING |
| Chain | Residue | Details |
| A | ASN95 | |
| B | ASN95 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) (high mannose) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:18191143, ECO:0000269|PubMed:27398304, ECO:0000269|PubMed:30296068, ECO:0000269|Ref.11, ECO:0000269|Ref.5, ECO:0000269|Ref.6, ECO:0000269|Ref.7, ECO:0007744|PDB:2E9E, ECO:0007744|PDB:2EFB, ECO:0007744|PDB:2EHA, ECO:0007744|PDB:2OJV, ECO:0007744|PDB:2R5L, ECO:0007744|PDB:3N8F, ECO:0007744|PDB:3NAK, ECO:0007744|PDB:3NIU, ECO:0007744|PDB:3QF1, ECO:0007744|PDB:3R55, ECO:0007744|PDB:3RKE, ECO:0007744|PDB:3SXV, ECO:0007744|PDB:4MSF, ECO:0007744|PDB:4OEK, ECO:0007744|PDB:4QJQ, ECO:0007744|PDB:5FF1, ECO:0007744|PDB:5HPW, ECO:0007744|PDB:6LF7, ECO:0007744|PDB:8ING |
| Chain | Residue | Details |
| A | ASN205 | |
| B | ASN205 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:18191143, ECO:0000269|PubMed:27398304, ECO:0000269|Ref.11, ECO:0000269|Ref.5, ECO:0000269|Ref.6, ECO:0000269|Ref.7, ECO:0007744|PDB:2E9E, ECO:0007744|PDB:2EFB, ECO:0007744|PDB:2EHA, ECO:0007744|PDB:2OJV, ECO:0007744|PDB:2R5L, ECO:0007744|PDB:3N8F, ECO:0007744|PDB:3NAK, ECO:0007744|PDB:3NIU, ECO:0007744|PDB:3QF1, ECO:0007744|PDB:3R55, ECO:0007744|PDB:3RKE, ECO:0007744|PDB:3SXV, ECO:0007744|PDB:4MSF, ECO:0007744|PDB:4OEK, ECO:0007744|PDB:4QJQ, ECO:0007744|PDB:5FF1, ECO:0007744|PDB:5HPW, ECO:0007744|PDB:6LF7, ECO:0007744|PDB:8ING |
| Chain | Residue | Details |
| A | ASN241 | |
| B | ASN241 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) (hybrid) asparagine; alternate => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:18191143, ECO:0000269|PubMed:27398304, ECO:0000269|PubMed:30296068, ECO:0000269|Ref.11, ECO:0000269|Ref.5, ECO:0000269|Ref.6, ECO:0000269|Ref.7, ECO:0007744|PDB:2E9E, ECO:0007744|PDB:2EFB, ECO:0007744|PDB:2EHA, ECO:0007744|PDB:2OJV, ECO:0007744|PDB:2R5L, ECO:0007744|PDB:3N8F, ECO:0007744|PDB:3NAK, ECO:0007744|PDB:3NIU, ECO:0007744|PDB:3QF1, ECO:0007744|PDB:3R55, ECO:0007744|PDB:3RKE, ECO:0007744|PDB:3SXV, ECO:0007744|PDB:4MSF, ECO:0007744|PDB:4OEK, ECO:0007744|PDB:4QJQ, ECO:0007744|PDB:5FF1, ECO:0007744|PDB:5HPW, ECO:0007744|PDB:6LF7, ECO:0007744|PDB:8ING |
| Chain | Residue | Details |
| A | ASN332 | |
| B | ASN332 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1mhl |
| Chain | Residue | Details |
| A | HIS109 | |
| A | ARG255 | |
| A | GLN105 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1mhl |
| Chain | Residue | Details |
| B | HIS109 | |
| B | ARG255 | |
| B | GLN105 |
