4L3T
Crystal Structure of Substrate-free Human Presequence Protease
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004222 | molecular_function | metalloendopeptidase activity |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0006508 | biological_process | proteolysis |
| A | 0006626 | biological_process | protein targeting to mitochondrion |
| A | 0008047 | molecular_function | enzyme activator activity |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0008237 | molecular_function | metallopeptidase activity |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051603 | biological_process | proteolysis involved in protein catabolic process |
| B | 0004222 | molecular_function | metalloendopeptidase activity |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0006508 | biological_process | proteolysis |
| B | 0006626 | biological_process | protein targeting to mitochondrion |
| B | 0008047 | molecular_function | enzyme activator activity |
| B | 0008233 | molecular_function | peptidase activity |
| B | 0008237 | molecular_function | metallopeptidase activity |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051603 | biological_process | proteolysis involved in protein catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1101 |
| Chain | Residue |
| A | HIS104 |
| A | HIS108 |
| A | GLU205 |
| A | ACT1108 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 1102 |
| Chain | Residue |
| A | SER453 |
| A | GOL1103 |
| A | HOH1208 |
| A | HOH1242 |
| A | GLY382 |
| A | TYR383 |
| A | SER449 |
| A | TYR450 |
| A | ALA452 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 1103 |
| Chain | Residue |
| A | TYR380 |
| A | GLY382 |
| A | GOL1102 |
| A | HOH1208 |
| A | HOH1404 |
| A | HOH1555 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT A 1104 |
| Chain | Residue |
| A | GLU214 |
| A | ASP373 |
| A | VAL378 |
| A | HOH1675 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT A 1105 |
| Chain | Residue |
| A | PHE210 |
| A | HIS220 |
| A | TYR510 |
| A | HOH1711 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACT A 1106 |
| Chain | Residue |
| A | CYS34 |
| A | LEU62 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 1107 |
| Chain | Residue |
| A | ARG36 |
| A | TYR40 |
| A | HIS78 |
| A | ALA80 |
| A | GLY269 |
| A | ASN270 |
| A | PHE271 |
| A | PRO272 |
| A | LEU273 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ACT A 1108 |
| Chain | Residue |
| A | HIS104 |
| A | GLN107 |
| A | HIS108 |
| A | ASN136 |
| A | ALA137 |
| A | GLU205 |
| A | TYR906 |
| A | ZN1101 |
| A | HOH1544 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 1101 |
| Chain | Residue |
| B | HIS104 |
| B | HIS108 |
| B | GLU205 |
| B | ACT1108 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 1102 |
| Chain | Residue |
| A | GLN682 |
| A | GLU686 |
| A | HOH1593 |
| A | HOH1594 |
| B | LEU629 |
| B | ASP631 |
| B | GLU634 |
| B | HOH1534 |
| site_id | BC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 1103 |
| Chain | Residue |
| B | GLY382 |
| B | TYR383 |
| B | SER449 |
| B | TYR450 |
| B | ALA452 |
| B | SER453 |
| B | GOL1104 |
| B | HOH1489 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 1104 |
| Chain | Residue |
| B | GLY382 |
| B | GOL1103 |
| B | HOH1324 |
| B | HOH1482 |
| B | HOH1485 |
| B | HOH1672 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT B 1105 |
| Chain | Residue |
| A | MLY794 |
| B | ASN358 |
| B | ASP423 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT B 1106 |
| Chain | Residue |
| B | SER56 |
| B | LEU62 |
| B | THR63 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT B 1107 |
| Chain | Residue |
| B | PHE210 |
| B | HIS220 |
| B | ASP238 |
| B | TYR510 |
| site_id | BC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ACT B 1108 |
| Chain | Residue |
| B | HIS104 |
| B | GLN107 |
| B | HIS108 |
| B | ALA137 |
| B | GLU205 |
| B | TYR906 |
| B | ZN1101 |
| B | HOH1525 |
| B | HOH1528 |
| site_id | BC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT B 1109 |
| Chain | Residue |
| B | ARG81 |
| B | ASP83 |
| B | SER440 |
| site_id | BC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT B 1110 |
| Chain | Residue |
| B | HOH1564 |
| A | LEU629 |
| A | GLU634 |
| B | ASN690 |
| B | HOH1563 |
| site_id | CC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT B 1111 |
| Chain | Residue |
| B | PRO926 |
| B | THR928 |
| B | ILE929 |
| B | GLU930 |
| site_id | CC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 1112 |
| Chain | Residue |
| B | HIS281 |
| B | ARG307 |
| B | HOH1398 |
| B | HOH1623 |
| site_id | CC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT B 1113 |
| Chain | Residue |
| A | GLN252 |
| A | THR256 |
| B | GLU527 |
| site_id | CC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT B 1114 |
| Chain | Residue |
| B | GLU214 |
| B | ASP373 |
| B | PHE374 |
| B | VAL378 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 60 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | Compositional bias: {"description":"Basic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"16849325","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24931469","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"UniProtKB","id":"Q9LJL3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"24931469","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4L3T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4NGE","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q8K411","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q8K411","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q8K411","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
