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4FKK

Crystal structure of porcine aminopeptidase-N complexed with bestatin

Functional Information from GO Data
ChainGOidnamespacecontents
A0001525biological_processangiogenesis
A0001618molecular_functionvirus receptor activity
A0004177molecular_functionaminopeptidase activity
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005886cellular_componentplasma membrane
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0030154biological_processcell differentiation
A0042277molecular_functionpeptide binding
A0043171biological_processpeptide catabolic process
A0046718biological_processsymbiont entry into host cell
A0046872molecular_functionmetal ion binding
A0070006molecular_functionmetalloaminopeptidase activity
Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VIAHELAHQW
ChainResidueDetails
AVAL380-TRP389

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10095
ChainResidueDetails
AGLU384

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P15144
ChainResidueDetails
AGLY347

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:22876187, ECO:0007744|PDB:4F5C
ChainResidueDetails
AHIS387
AGLU406
AHIS383

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000250|UniProtKB:P15144
ChainResidueDetails
ATYR472

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Sulfotyrosine => ECO:0000255
ChainResidueDetails
ATYR171

site_idSWS_FT_FI6
Number of Residues10
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22876187, ECO:0007744|PDB:4F5C
ChainResidueDetails
AASN314
AASN328
AASN506
AASN622
AASN646
AASN736
AASN82
AASN124
AASN229
AASN237

site_idSWS_FT_FI7
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN258
AASN286
AASN556
AASN569

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PDB entries from 2024-05-15

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