Structure of PDB 6a8z Chain B

Receptor sequence
>6a8zB (length=431) Species: 243230 (Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539) [Search protein sequence]
QSVGDSIFPSLGQRGLDVQHYDLHLTVPRPGEPHLSGDVTLTVGAREPLS
RIVLDLLGPRVSAAQWNGQRVRWVQTAQKVEVTLPRPLRPGETGRLRLIY
AGTPELSPGLPIRPGWQNEAGLSYSLSEPHGTRGFLPCNDHPSDPATFTV
RVTVPASASAAASGLFTTQTERNGLKTLTFTQRVPVPTYALGLIVGPLER
RTAPDVQLGTQTVHRRDIYAAGLPAGTTVPEGETARMLRVLSDWFGPYPD
EVYGVALLPVRQLALETAGLTTMPATSNRERVRLHELAHQWFGDQVTLAD
WADTWLSEGFATYAELLWAESQGEDGQAMAADWYARLSVLPSRPLRATRE
EEIFDASAYFRGALALHALRLKVGDAAFGQFLHSYVKTFTGRPVSTTALL
TLVKTQLGAEAEQTLRVWVEGRTLPPLPEPV
3D structure
PDB6a8z Two-domain aminopeptidase of M1 family: Structural features for substrate binding and gating in absence of C-terminal domain.
ChainB
Resolution2.045 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 E323 H326 E345 E388 Y396
Catalytic site (residue number reindexed from 1) E266 H285 E286 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 ZN B H322 H326 E345 H285 H289 E308
BS02 TYR B I149 E165 A301 E303 H322 H326 E345 Y396 I112 E128 A264 E266 H285 H289 E308 Y359
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:6a8z, PDBe:6a8z, PDBj:6a8z
PDBsum6a8z
PubMed31351924
UniProtQ9RVZ5

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