Structure of PDB 5lds Chain D

Receptor sequence
>5ldsD (length=898) Species: 9823 (Sus scrofa) [Search protein sequence]
QSKPWNRYRLPTTLLPDSYNVTLRPYLTPNADGLYIFKGKSIVRFICQEP
TDVIIIHSKKLNYTHMVVLRGVGDSQVPEIDRTELVELTEYLVVHLKGSL
QPGHMYEMESEFQGELADDLAGFYRSEYMEGNVKKVLATTQMQSTDARKS
FPCFDEPAMKATFNITLIHPNNLTALSNMPPKGSSTPLAEDPNWSVTEFE
TTPVMSTYLLAYIVSEFQSVNETAQNGVLIRIWARPNAIAEGHGMYALNV
TGPILNFFANHYNTSYPLPKSDQIALPDFNAGAMENWGLVTYRENALLFD
PQSSSISNKERVVTVIAHELAHQWFGNLVTLAWWNDLWLNEGFASYVEYL
GADHAEPTWNLKDLIVPGDVYRVMAVDALASSHPLTTPAEEVNTPAQISE
MFDSISYSKGASVIRMLSNFLTEDLFKEGLASYLHAFAYQNTTYLDLWEH
LQKAVDAQTSIRLPDTVRAIMDRWTLQMGFPVITVDTKTGNISQKHFLLD
SESNVTRSSAFDYLWIVPISSIKNGVMQDHYWLRDVSQAQNDLFKTASDD
WVLLNVNVTGYFQVNYDEDNWRMIQHQLQTNLSVIPVINRAQVIYDSFNL
ATAHMVPVTLALDNTLFLNGEKEYMPWQAALSSLSYFSLMFDRSEVYGPM
KKYLRKQVEPLFQHFETLTKNWTERPENLMDQYSEINAISTACSNGLPQC
ENLAKTLFDQWMSDPENNPIHPNLRSTIYCNAIAQGGQDQWDFAWGQLQQ
AQLVNEADKLRSALACSNEVWLLNRYLGYTLNPDLIRKQDATSTINSIAS
NVIGQPLAWDFVQSNWKKLFQDYGGGSFSFSNLIQGVTRRFSSEFELQQL
EQFKKNNMDVGFGSGTRALEQALEKTKANIKWVKENKEVVLNWFIEHS
3D structure
PDB5lds Allosteric inhibition of aminopeptidase N functions related to tumor growth and virus infection.
ChainD
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E350 H383 E384 H387 E406 S464 Y472
Catalytic site (residue number reindexed from 1) E285 H318 E319 H322 E341 S399 Y407
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 BMA D T288 A289 T223 A224
BS02 BMA D Q290 G292 Q225 G227
BS03 ZN D H383 H387 E406 H318 H322 E341
Gene Ontology
Molecular Function
GO:0001618 virus receptor activity
GO:0004177 aminopeptidase activity
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
GO:0042277 peptide binding
GO:0046872 metal ion binding
GO:0070006 metalloaminopeptidase activity
Biological Process
GO:0001525 angiogenesis
GO:0006508 proteolysis
GO:0030154 cell differentiation
GO:0043171 peptide catabolic process
GO:0046718 symbiont entry into host cell
Cellular Component
GO:0005615 extracellular space
GO:0005737 cytoplasm
GO:0005886 plasma membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5lds, PDBe:5lds, PDBj:5lds
PDBsum5lds
PubMed28393915
UniProtP15145|AMPN_PIG Aminopeptidase N (Gene Name=ANPEP)

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