Structure of PDB 1u4g Chain A

Receptor sequence
>1u4gA (length=298) Species: 287 (Pseudomonas aeruginosa) [Search protein sequence]
AEAGGPGGNQKIGKYTYGSDYGPLIVNDRCEMDDGNVITVDMNSSTDDSK
TTPFRFACPTNTYKQVNGAYSPLNDAHFFGGVVFKLYRDWFGTSPLTHKL
YMKVHYGRSVENAYWDGTAMLFGDGATMFYPLVSLDVAAHEVSHGFTEQN
SGLIYRGQSGGMNEAFSDMAGEAAEFYMRGKNDFLIGYDIKKGSGALRYM
DQPSRDGRSIDNASQYYNGIDVHHSSGVYNRAFYLLANSPGWDTRKAFEV
FVDANRYYWTATSNYNSGACGVIRSAQNRNYSAADVTRAFSTVGVTCP
3D structure
PDB1u4g Structural comparison suggests that thermolysin and related neutral proteases undergo hinge-bending motion during catalysis
ChainA
Resolution1.4 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) H140 E141 H144 Y155 E164 D221 H223
Catalytic site (residue number reindexed from 1) H140 E141 H144 Y155 E164 D221 H223
Enzyme Commision number 3.4.24.26: pseudolysin.
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 ZN A H140 H144 E164 H140 H144 E164
BS02 CA A D136 E172 E175 D183 L185 D136 E172 E175 D183 L185
BS03 HPI A N112 A113 Y114 V137 H140 E141 H144 E164 I186 L197 R198 H223 N112 A113 Y114 V137 H140 E141 H144 E164 I186 L197 R198 H223
Gene Ontology
Molecular Function
GO:0004222 metalloendopeptidase activity
Biological Process
GO:0006508 proteolysis

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1u4g, PDBe:1u4g, PDBj:1u4g
PDBsum1u4g
PubMed
UniProtP14756|ELAS_PSEAE Elastase (Gene Name=lasB)

[Back to BioLiP]