Structure of PDB 6iff Chain A

Receptor sequence
>6iffA (length=429) Species: 243230 (Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539) [Search protein sequence]
QSVGDSIFPSLGQRGLDVQHYDLHLTVPRPGEPHLSGDVTLTVGAREPLS
RIVLDLLGPRVSAAQWNGQRVRWVQTAQKVEVTLPRPLRPGETGRLRLIY
AGTPELSGLPIRPGWQNEAGLSYSLSEPHGTRGFLPCNDHPSDPATFTVR
VTVPASASAAASGLFTTQTERNGLKTLTFTQRVPVPTYALGLIVGPLERR
TAPDVQLGTQTVHRRDIYAAGLPAGTTVPEGETARMLRVLSDWFGPYPDE
VYGVALLPVRQLALETAGLTTMPATSNRERVRLHALAHQWFGDQVTLADW
ADTWLSEGFATYAELLWAESQGEDGQAMAADWYARLSVLPSRPLRATREE
EIFDASAYFRGALALHALRLKVGDAAFGQFLHSYVKTFTGRPVSTTALLT
LVKTQLGAEAEQTLRVWVEGRTLPPLPEP
3D structure
PDB6iff Structural basis for the unusual substrate specificity of unique two-domain M1 metallopeptidase.
ChainA
Resolution1.83 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) E265 H284 A285 H288 E307 E350 Y358
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 H284 H288 E307
BS02 TYR A I149 E165 A301 E303 H322 H326 E345 F391 Y396 I111 E127 A263 E265 H284 H288 E307 F353 Y358
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:6iff, PDBe:6iff, PDBj:6iff
PDBsum6iff
PubMed31923495
UniProtQ9RVZ5

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