5NI4
Crystal structure of human LTA4H mutant E271A in complex with LTA4 (crystal form II)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003723 | molecular_function | RNA binding |
A | 0004177 | molecular_function | aminopeptidase activity |
A | 0004301 | molecular_function | epoxide hydrolase activity |
A | 0004463 | molecular_function | leukotriene-A4 hydrolase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005576 | cellular_component | extracellular region |
A | 0005634 | cellular_component | nucleus |
A | 0005654 | cellular_component | nucleoplasm |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006508 | biological_process | proteolysis |
A | 0006629 | biological_process | lipid metabolic process |
A | 0006691 | biological_process | leukotriene metabolic process |
A | 0008233 | molecular_function | peptidase activity |
A | 0008237 | molecular_function | metallopeptidase activity |
A | 0008270 | molecular_function | zinc ion binding |
A | 0010043 | biological_process | response to zinc ion |
A | 0019370 | biological_process | leukotriene biosynthetic process |
A | 0019538 | biological_process | protein metabolic process |
A | 0043171 | biological_process | peptide catabolic process |
A | 0043434 | biological_process | response to peptide hormone |
A | 0045148 | molecular_function | tripeptide aminopeptidase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0060509 | biological_process | type I pneumocyte differentiation |
A | 0070006 | molecular_function | metalloaminopeptidase activity |
A | 0070062 | cellular_component | extracellular exosome |
A | 1904724 | cellular_component | tertiary granule lumen |
A | 1904813 | cellular_component | ficolin-1-rich granule lumen |
B | 0003723 | molecular_function | RNA binding |
B | 0004177 | molecular_function | aminopeptidase activity |
B | 0004301 | molecular_function | epoxide hydrolase activity |
B | 0004463 | molecular_function | leukotriene-A4 hydrolase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005576 | cellular_component | extracellular region |
B | 0005634 | cellular_component | nucleus |
B | 0005654 | cellular_component | nucleoplasm |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006508 | biological_process | proteolysis |
B | 0006629 | biological_process | lipid metabolic process |
B | 0006691 | biological_process | leukotriene metabolic process |
B | 0008233 | molecular_function | peptidase activity |
B | 0008237 | molecular_function | metallopeptidase activity |
B | 0008270 | molecular_function | zinc ion binding |
B | 0010043 | biological_process | response to zinc ion |
B | 0019370 | biological_process | leukotriene biosynthetic process |
B | 0019538 | biological_process | protein metabolic process |
B | 0043171 | biological_process | peptide catabolic process |
B | 0043434 | biological_process | response to peptide hormone |
B | 0045148 | molecular_function | tripeptide aminopeptidase activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0060509 | biological_process | type I pneumocyte differentiation |
B | 0070006 | molecular_function | metalloaminopeptidase activity |
B | 0070062 | cellular_component | extracellular exosome |
B | 1904724 | cellular_component | tertiary granule lumen |
B | 1904813 | cellular_component | ficolin-1-rich granule lumen |
C | 0003723 | molecular_function | RNA binding |
C | 0004177 | molecular_function | aminopeptidase activity |
C | 0004301 | molecular_function | epoxide hydrolase activity |
C | 0004463 | molecular_function | leukotriene-A4 hydrolase activity |
C | 0005515 | molecular_function | protein binding |
C | 0005576 | cellular_component | extracellular region |
C | 0005634 | cellular_component | nucleus |
C | 0005654 | cellular_component | nucleoplasm |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0006508 | biological_process | proteolysis |
C | 0006629 | biological_process | lipid metabolic process |
C | 0006691 | biological_process | leukotriene metabolic process |
C | 0008233 | molecular_function | peptidase activity |
C | 0008237 | molecular_function | metallopeptidase activity |
C | 0008270 | molecular_function | zinc ion binding |
C | 0010043 | biological_process | response to zinc ion |
C | 0019370 | biological_process | leukotriene biosynthetic process |
C | 0019538 | biological_process | protein metabolic process |
C | 0043171 | biological_process | peptide catabolic process |
C | 0043434 | biological_process | response to peptide hormone |
C | 0045148 | molecular_function | tripeptide aminopeptidase activity |
C | 0046872 | molecular_function | metal ion binding |
C | 0060509 | biological_process | type I pneumocyte differentiation |
C | 0070006 | molecular_function | metalloaminopeptidase activity |
C | 0070062 | cellular_component | extracellular exosome |
C | 1904724 | cellular_component | tertiary granule lumen |
C | 1904813 | cellular_component | ficolin-1-rich granule lumen |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue ZN A 701 |
Chain | Residue |
A | HIS295 |
A | HIS299 |
A | GLU318 |
A | DJ3705 |
A | HOH804 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue IMD A 702 |
Chain | Residue |
A | GLN508 |
A | HOH1206 |
A | GLY344 |
A | GLY347 |
A | GLU348 |
A | GLU501 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue IMD A 703 |
Chain | Residue |
A | GLY248 |
A | PRO250 |
A | VAL252 |
A | GLU412 |
A | SER415 |
A | HOH1002 |
A | HOH1152 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue IMD A 704 |
Chain | Residue |
A | ASP422 |
A | ASP426 |
A | HOH1004 |
A | HOH1385 |
site_id | AC5 |
Number of Residues | 20 |
Details | binding site for residue DJ3 A 705 |
Chain | Residue |
A | GLN136 |
A | ALA137 |
A | TYR267 |
A | GLY268 |
A | GLY269 |
A | MET270 |
A | HIS295 |
A | GLU296 |
A | TRP311 |
A | PHE314 |
A | GLU318 |
A | VAL367 |
A | TYR378 |
A | TYR383 |
A | ARG563 |
A | ZN701 |
A | HOH801 |
A | HOH804 |
A | HOH810 |
A | HOH1145 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue ZN B 701 |
Chain | Residue |
B | HIS295 |
B | HIS299 |
B | GLU318 |
B | DJ3705 |
B | HOH808 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue IMD B 702 |
Chain | Residue |
B | GLY344 |
B | GLY347 |
B | GLU348 |
B | GLU501 |
B | ALA504 |
B | GLN508 |
site_id | AC8 |
Number of Residues | 2 |
Details | binding site for residue IMD B 703 |
Chain | Residue |
B | ASP422 |
B | ASP426 |
site_id | AC9 |
Number of Residues | 10 |
Details | binding site for residue IMD B 704 |
Chain | Residue |
B | GLY248 |
B | GLY249 |
B | PRO250 |
B | LEU305 |
B | VAL411 |
B | GLU412 |
B | SER415 |
B | HOH896 |
B | HOH988 |
B | HOH1063 |
site_id | AD1 |
Number of Residues | 21 |
Details | binding site for residue DJ3 B 705 |
Chain | Residue |
B | GLN136 |
B | ALA137 |
B | TYR267 |
B | GLY268 |
B | GLY269 |
B | HIS295 |
B | GLU296 |
B | HIS299 |
B | TRP311 |
B | PHE314 |
B | GLU318 |
B | VAL367 |
B | PRO374 |
B | TYR378 |
B | TYR383 |
B | ARG563 |
B | LYS565 |
B | ZN701 |
B | HOH808 |
B | HOH870 |
B | HOH1007 |
site_id | AD2 |
Number of Residues | 5 |
Details | binding site for residue ZN C 701 |
Chain | Residue |
C | HIS295 |
C | HIS299 |
C | GLU318 |
C | DJ3703 |
C | HOH805 |
site_id | AD3 |
Number of Residues | 7 |
Details | binding site for residue IMD C 702 |
Chain | Residue |
C | GLY344 |
C | GLY347 |
C | GLU348 |
C | ASN351 |
C | GLU501 |
C | ALA504 |
C | GLN508 |
site_id | AD4 |
Number of Residues | 22 |
Details | binding site for residue DJ3 C 703 |
Chain | Residue |
C | ALA137 |
C | TYR267 |
C | GLY268 |
C | GLY269 |
C | MET270 |
C | HIS295 |
C | GLU296 |
C | TRP311 |
C | PHE314 |
C | GLU318 |
C | VAL367 |
C | PRO374 |
C | TYR383 |
C | ARG563 |
C | LYS565 |
C | ZN701 |
C | HOH805 |
C | HOH865 |
C | HOH1025 |
C | HOH1169 |
C | HOH1203 |
C | GLN136 |
Functional Information from PROSITE/UniProt
site_id | PS00142 |
Number of Residues | 10 |
Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VIAHEISHSW |
Chain | Residue | Details |
A | VAL292-TRP301 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:11675384, ECO:0000305|PubMed:12207002, ECO:0000305|PubMed:24591641, ECO:0007744|PDB:1H19 |
Chain | Residue | Details |
A | GLU296 | |
B | GLU296 | |
C | GLU296 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | ACT_SITE: Proton donor => ECO:0000269|PubMed:11675384, ECO:0000305|PubMed:12207002, ECO:0000305|PubMed:24591641, ECO:0007744|PDB:1H19 |
Chain | Residue | Details |
A | TYR383 | |
B | TYR383 | |
C | TYR383 |
site_id | SWS_FT_FI3 |
Number of Residues | 9 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18804029 |
Chain | Residue | Details |
A | GLN134 | |
A | PRO266 | |
A | ARG563 | |
B | GLN134 | |
B | PRO266 | |
B | ARG563 | |
C | GLN134 | |
C | PRO266 | |
C | ARG563 |
Chain | Residue | Details |
A | HIS295 | |
A | HIS299 | |
B | HIS295 | |
B | HIS299 | |
C | HIS295 | |
C | HIS299 |
Chain | Residue | Details |
A | GLU318 | |
B | GLU318 | |
C | GLU318 |
site_id | SWS_FT_FI6 |
Number of Residues | 6 |
Details | SITE: Pro-Gly-Pro binding => ECO:0000269|PubMed:24591641 |
Chain | Residue | Details |
A | ALA271 | |
A | GLY562 | |
B | ALA271 | |
B | GLY562 | |
C | ALA271 | |
C | GLY562 |
site_id | SWS_FT_FI7 |
Number of Residues | 3 |
Details | SITE: Essential for epoxide hydrolase activity, but not for aminopeptidase activity => ECO:0000269|PubMed:11917124 |
Chain | Residue | Details |
A | ASP375 | |
B | ASP375 | |
C | ASP375 |
site_id | SWS_FT_FI8 |
Number of Residues | 3 |
Details | SITE: Covalently modified during suicide inhibition by leukotrienes => ECO:0000269|PubMed:7667299 |
Chain | Residue | Details |
A | TYR378 | |
B | TYR378 | |
C | TYR378 |
site_id | SWS_FT_FI9 |
Number of Residues | 12 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS72 | |
C | LYS336 | |
C | LYS413 | |
C | LYS572 | |
A | LYS336 | |
A | LYS413 | |
A | LYS572 | |
B | LYS72 | |
B | LYS336 | |
B | LYS413 | |
B | LYS572 | |
C | LYS72 |
site_id | SWS_FT_FI10 |
Number of Residues | 3 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:9395533 |
Chain | Residue | Details |
A | SER415 | |
B | SER415 | |
C | SER415 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 7 |
Details | M-CSA 166 |
Chain | Residue | Details |
A | ALA271 | electrostatic stabiliser, hydrogen bond acceptor, nucleofuge, nucleophile |
A | HIS295 | metal ligand |
A | GLU296 | electrostatic stabiliser |
A | HIS299 | metal ligand |
A | GLU318 | metal ligand |
A | ASP375 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | TYR383 | electrostatic stabiliser |
site_id | MCSA2 |
Number of Residues | 7 |
Details | M-CSA 166 |
Chain | Residue | Details |
B | ALA271 | electrostatic stabiliser, hydrogen bond acceptor, nucleofuge, nucleophile |
B | HIS295 | metal ligand |
B | GLU296 | electrostatic stabiliser |
B | HIS299 | metal ligand |
B | GLU318 | metal ligand |
B | ASP375 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | TYR383 | electrostatic stabiliser |
site_id | MCSA3 |
Number of Residues | 7 |
Details | M-CSA 166 |
Chain | Residue | Details |
C | ALA271 | electrostatic stabiliser, hydrogen bond acceptor, nucleofuge, nucleophile |
C | HIS295 | metal ligand |
C | GLU296 | electrostatic stabiliser |
C | HIS299 | metal ligand |
C | GLU318 | metal ligand |
C | ASP375 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
C | TYR383 | electrostatic stabiliser |