Structure of PDB 2rmp Chain A

Receptor sequence
>2rmpA (length=358) Species: 4839 (Rhizomucor miehei) [Search protein sequence]
DGSVDTPGYYDFDLEEYAIPVSIGTPGQDFLLLFDTGSSDTWVPHKGCTK
SEGCVGSRFFDPSASSTFKATNYNLNITYGTGGANGLYFEDSIAIGDITV
TKQILAYVDNVRGPTAEQSPNADIFLDGLFGAAYPDNTAMEAEYGSTYNT
VHVNLYKQGLISSPLFSVYMNTNSGTGEVVFGGVNNTLLGGDIAYTDVMS
RYGGYYFWDAPVTGITVDGSAAVRFSRPQAFTIDTGTNFFIMPSSAASKI
VKAALPDATETQQGWVVPCASYQNSKSTISIVMQKSGSSSDTIEISVPVS
KMLLPVDQSNETCMFIILPDGGNQYIVGNLFLRFFVNVYDFGNNRIGFAP
LASAYENE
3D structure
PDB2rmp Structure of the Rhizomucor miehei aspartic proteinase complexed with the inhibitor pepstatin A at 2.7 A resolution.
ChainA
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) D38 S41 D43 W45 Y82 D237 T240
Catalytic site (residue number reindexed from 1) D35 S38 D40 W42 Y79 D234 T237
Enzyme Commision number 3.4.23.23: mucorpepsin.
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 L36 D38 G40 Y82 G83 T84 P117 F210 D237 T240 N241 L321 I329 L33 D35 G37 Y79 G80 T81 P114 F207 D234 T237 N238 L318 I326
Gene Ontology
Molecular Function
GO:0004190 aspartic-type endopeptidase activity
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:2rmp, PDBe:2rmp, PDBj:2rmp
PDBsum2rmp
PubMed10089458
UniProtP00799|CARP_RHIMI Mucorpepsin

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