Structure of PDB 6koz Chain A

Receptor sequence
>6kozA (length=436) Species: 243230 (Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539) [Search protein sequence]
QSVGDSIFPSLGQRGLDVQHYDLHLTVPRPGEPHLSGDVTLTVGAREPLS
RIVLDLLGPRVSAAQWNGQRVRWVQTAQKVEVTLPRPLRPGETGRLRLIY
AGTPELSGDPGLPIRPGWQNEAGLSYSLSEPHGTRGFLPCNDHPSDPATF
TVRVTVPASASAAASGLFTTQTERNGLKTLTFTQRVPVPTYALGLIVGPL
ERRTAPDVQLGTQTVHRRDIYAAGLPAGTTVPEGETARMLRVLSDWFGPY
PDEVYGVALLPVRQLALETAGLTTMPATSNRERVRLHALAHQWFGDQVTL
ADWADTWLSEGFATYAELLWAESQGEDGQAMAADWYARLSVLPSRPLRAT
REEEIFDASAYFRGALALHALRLKVGDAAFGQFLHSYVKTFTGRPVSTTA
LLTLVKTQLGAEAEQTLRVWVEGRTLPPLPEPVGAP
3D structure
PDB6koz Structural basis for the unusual substrate specificity of unique two-domain M1 metallopeptidase.
ChainA
Resolution2.25 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E303 H322 A323 H326 E345 E388 Y396
Catalytic site (residue number reindexed from 1) E268 H287 A288 H291 E310 E353 Y361
Enzyme Commision number 3.4.11.2: membrane alanyl aminopeptidase.
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 H322 H326 E345 H287 H291 E310
BS02 LEU A E165 A301 E345 Y396 E130 A266 E310 Y361
Gene Ontology
Molecular Function
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:6koz, PDBe:6koz, PDBj:6koz
PDBsum6koz
PubMed31923495
UniProtQ9RVZ5

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