Structure of PDB 6kp0 Chain A

Receptor sequence
>6kp0A (length=432) Species: 243230 (Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539) [Search protein sequence]
QSVGDSIFPSLGQRGLDVQHYDLHLTVPRPGEPHLSGDVTLTVGAREPLS
RIVLDLLGPRVSAAQWNGQRVRWVQTAQKVEVTLPRPLRPGETGRLRLIY
AGTPELSGDPLPIRPGWQNEAGLSYSLSEPHGTRGFLPCNDHPSDPATFT
VRVTVPASASAAASGLFTTQTERNGLKTLTFTQRVPVPTYALGLIVGPLE
RRTAPDVQLGTQTVHRRDIYAAGLPAGTTVPEGETARMLRVLSDWFGPYP
DEVYGVALLPVRQLALETAGLTTMPATSNRERVRLHALAHQWFGDQVTLA
DWADTWLSEGFATYAELLWAESQGEDGQAMAADWYARLSVLPSRPLRATR
EEEIFDASAYFRGALALHALRLKVGDAAFGQFLHSYVKTFTGRPVSTTAL
LTLVKTQLGAEAEQTLRVWVEGRTLPPLPEPV
3D structure
PDB6kp0 Structural basis for the unusual substrate specificity of unique two-domain M1 metallopeptidase.
ChainA
Resolution2.1 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) E267 H286 A287 H290 E309 E352 Y360
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 H286 H290 E309
BS02 ARG A P148 E165 A301 L302 E303 H322 H326 F391 Y396 P112 E129 A265 L266 E267 H286 H290 F355 Y360
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:6kp0, PDBe:6kp0, PDBj:6kp0
PDBsum6kp0
PubMed31923495
UniProtQ9RVZ5

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