Structure of PDB 1gbi Chain A

Receptor sequence
>1gbiA (length=198) Species: 69 (Lysobacter enzymogenes) [Search protein sequence]
ANIVGGIEYSINNASLCSVGFSVTRGATKGFVTAGHCGTVNATARIGGAV
VGTFAARVFPGNDRAWVSLTSAQTLLPRVANGSSFVTVRGSTEAAVGAAV
CRSGRTTGYQCGTITAKNVTANYAEGAVRGLTQGNACAGRGDSGGSWITS
AGQAQGVMSGLNVQSNGNNCGIPASQRSSLFERLQPILSQYGLSLVTG
3D structure
PDB1gbi Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity.
ChainA
Resolution2.3 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) H57 D102 G193 S195 S214
Catalytic site (residue number reindexed from 1) H36 D63 G141 S143 S159
Enzyme Commision number 3.4.21.12: alpha-lytic endopeptidase.
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 peptide A H57 Y171 R192 S195 S214 G215 L216 V218 H36 Y123 R140 S143 S159 G160 L161 V163
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
Biological Process
GO:0006508 proteolysis

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1gbi, PDBe:1gbi, PDBj:1gbi
PDBsum1gbi
PubMed7500345
UniProtP00778|PRLA_LYSEN Alpha-lytic protease (Gene Name=alpha-LP)

[Back to BioLiP]