Structure of PDB 3hdi Chain B

Receptor sequence
>3hdiB (length=414) Species: 272558 (Halalkalibacterium halodurans C-125) [Search protein sequence]
INTMTLDNGVRIITEKMSTVRSVSIGIWVGTGSRYESAEENGISHFLEHM
FFKGTNTRSAQEIAEFFDSIGGQVNAFTSKEYTCYYAKVLDDHAGQAIDT
LSDMFFHSTFQKEELEKERKVVFEEIKMVDDTPDDIVHDLLSSATYGKHS
LGYPILGTVETLNSFNEGMLRHYMDRFYTGDYVVISVAGNVHDELIDKIK
ETFSQVKPTTYNYQGEKPMFLPNRIVRKKETEQAHLCLGYPGLPIGDKDV
YALVLLNNVLGGSMSSRLFQDIREKRGLCYSVFSYHSSFRDSGMLTIYAG
TGHDQLDDLVYSIQETTSALAEKGLTEKELENGKEQLKGSLMLSLESTNS
RMSRNGKNELLLKKHRSLDEMIEQINAVQKQDVSRLAKILLSASPSISLI
NANGELPKALIHLE
3D structure
PDB3hdi Crystal and solution structures of a prokaryotic M16B peptidase: an open and shut case.
ChainB
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H46 E49 H50 E119 E126
Catalytic site (residue number reindexed from 1) H45 E48 H49 E118 E125
Enzyme Commision number ?
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 B R274 Y281 S282 R273 Y280 S281
BS02 peptide B E49 H50 N76 A77 F78 E126 D136 H139 D140 Y286 S348 N350 S354 E48 H49 N75 A76 F77 E125 D135 H138 D139 Y285 S347 N349 S353
BS03 CO B H46 H50 E126 H45 H49 E125
Gene Ontology
Molecular Function
GO:0004222 metalloendopeptidase activity
GO:0008233 peptidase activity
GO:0042802 identical protein 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:3hdi, PDBe:3hdi, PDBj:3hdi
PDBsum3hdi
PubMed19913481
UniProtQ9KA85

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