Structure of PDB 6ifg Chain A

Receptor sequence
>6ifgA (length=430) Species: 243230 (Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539) [Search protein sequence]
QSVGDSIFPSLGQRGLDVQHYDLHLTVPRPGEPHLSGDVTLTVGAREPLS
RIVLDLLGPRVSAAQWNGQRVRWVQTAQKVEVTLPRPLRPGETGRLRLIY
AGTPELDPGLPIRPGWQNEAGLSYSLSEPHGTRGFLPCNDHPSDPATFTV
RVTVPASASAAASGLFTTQTERNGLKTLTFTQRVPVPTYALGLIVGPLER
RTAPDVQLGTQTVHRRDIYAAGLPAGTTVPEGETARMLRVLSDWFGPYPD
EVYGVALLPVRQLALETAGLTTMPATSNRERVRLHALAHQWFGDQVTLAD
WADTWLSEGFATYAELLWAESQGEDGQAMAADWYARLSVLPSRPLRATRE
EEIFDASAYFRGALALHALRLKVGDAAFGQFLHSYVKTFTGRPVSTTALL
TLVKTQLGAEAEQTLRVWVEGRTLPPLPEP
3D structure
PDB6ifg Two-domain aminopeptidase of M1 family: Structural features for substrate binding and gating in absence of C-terminal domain.
ChainA
Resolution1.9 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) E266 H285 A286 H289 E308 E351 Y359
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 peptide A E165 L300 A301 L302 S314 R316 V319 H322 E345 F391 Y396 E128 L263 A264 L265 S277 R279 V282 H285 E308 F354 Y359
BS02 ZN A H322 H326 E345 H285 H289 E308
BS03 ZN A D52 V53 D181 D17 V18 D144
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:6ifg, PDBe:6ifg, PDBj:6ifg
PDBsum6ifg
PubMed31351924
UniProtQ9RVZ5

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