Structure of PDB 4lvn Chain A

Receptor sequence
>4lvnA (length=336) Species: 5833 (Plasmodium falciparum) [Search protein sequence]
HFNDEFRNLQWGLDLSRLDETQELINEHQVMSTRICVIDSGIDYNHPDLK
DNIELNLKELHGRKGFDDDNNGIVDDIYGANFVNNSGNPMDDNYHGTHVS
GIISAIGNNNIGVVGVDVNSKLIICKALDEHKLGRLGDMFKCLDYCISRN
AHMINGSFSFDEYSGIFNSSVEYLQRKGILFFVSASNCSHPKSSTPDIRK
CDLSINAKYPPILSTVYDNVISVANLKKNDNNNHYSLSINSFYSNKYCQL
AAPGTNIYSTAPHNSYRKLNGTSMAAPHVAAIASLIFSINPDLSYKKVIQ
ILKDSIVYLPSLKNMVAWAGYADINKAVNLAIKSKK
3D structure
PDB4lvn The malaria parasite egress protease SUB1 is a calcium-dependent redox switch subtilisin.
ChainA
Resolution2.25 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D372 H428 N520 S606
Catalytic site (residue number reindexed from 1) D39 H95 N187 S273
Enzyme Commision number 3.4.21.62: subtilisin.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 CA A E338 D381 I439 N442 I444 V446 E5 D48 I106 N109 I111 V113
BS02 CA A E392 R396 F399 D401 D408 E59 R63 F66 D68 D75
BS03 CA A E392 D400 D402 N404 I406 D409 E59 D67 D69 N71 I73 D76
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0008236 serine-type peptidase activity
Biological Process
GO:0006508 proteolysis

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4lvn, PDBe:4lvn, PDBj:4lvn
PDBsum4lvn
PubMed24785947
UniProtO61142|SUB1_PLAFA Subtilisin-like protease 1 (Gene Name=SUB1)

[Back to BioLiP]