Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4KXA

Crystal structure of human aminopeptidase A complexed with aspartate and calcium

Functional Information from GO Data
ChainGOidnamespacecontents
A0001525biological_processangiogenesis
A0002003biological_processangiotensin maturation
A0003081biological_processregulation of systemic arterial blood pressure by renin-angiotensin
A0004177molecular_functionaminopeptidase activity
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005765cellular_componentlysosomal membrane
A0005886cellular_componentplasma membrane
A0005903cellular_componentbrush border
A0006508biological_processproteolysis
A0007267biological_processcell-cell signaling
A0008217biological_processregulation of blood pressure
A0008233molecular_functionpeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0008283biological_processcell population proliferation
A0009897cellular_componentexternal side of plasma membrane
A0016324cellular_componentapical plasma membrane
A0016477biological_processcell migration
A0031410cellular_componentcytoplasmic vesicle
A0032835biological_processglomerulus development
A0042277molecular_functionpeptide binding
A0043171biological_processpeptide catabolic process
A0045177cellular_componentapical part of cell
A0046872molecular_functionmetal ion binding
A0070006molecular_functionmetalloaminopeptidase activity
A0070062cellular_componentextracellular exosome
Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VVAHELVHQW
ChainResidueDetails
AVAL390-TRP399

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:23888046, ECO:0007744|PDB:4KXB, ECO:0007744|PDB:4KXD
ChainResidueDetails
AGLU394

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:23888046, ECO:0007744|PDB:4KX9, ECO:0007744|PDB:4KXA, ECO:0007744|PDB:4KXB
ChainResidueDetails
AGLU223

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:23888046, ECO:0007744|PDB:4KXA, ECO:0007744|PDB:4KXB, ECO:0007744|PDB:4KXC, ECO:0007744|PDB:4KXD
ChainResidueDetails
AGLY357

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:23888046, ECO:0007744|PDB:4KX7, ECO:0007744|PDB:4KX8, ECO:0007744|PDB:4KX9, ECO:0007744|PDB:4KXA, ECO:0007744|PDB:4KXB, ECO:0007744|PDB:4KXC, ECO:0007744|PDB:4KXD
ChainResidueDetails
AHIS397
AGLU416
AHIS393

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:23888046, ECO:0007744|PDB:4KXA, ECO:0007744|PDB:4KXC, ECO:0007744|PDB:4KXD
ChainResidueDetails
AARG887

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Binds calcium which modulates its enzyme activity => ECO:0000269|PubMed:23888046
ChainResidueDetails
AASP221

site_idSWS_FT_FI7
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000269|PubMed:23888046, ECO:0007744|PDB:4KX9, ECO:0007744|PDB:4KXA, ECO:0007744|PDB:4KXB, ECO:0007744|PDB:4KXC, ECO:0007744|PDB:4KXD
ChainResidueDetails
ATYR479

site_idSWS_FT_FI8
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine; atypical => ECO:0000269|PubMed:23888046, ECO:0007744|PDB:4KX7
ChainResidueDetails
AASN98

site_idSWS_FT_FI9
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN124
AASN773

site_idSWS_FT_FI10
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:23888046, ECO:0007744|PDB:4KX7, ECO:0007744|PDB:4KX8, ECO:0007744|PDB:4KX9, ECO:0007744|PDB:4KXA, ECO:0007744|PDB:4KXB, ECO:0007744|PDB:4KXC, ECO:0007744|PDB:4KXD
ChainResidueDetails
AASN197
AASN678
AASN801
AASN828

site_idSWS_FT_FI11
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:23888046, ECO:0007744|PDB:4KX7, ECO:0007744|PDB:4KX8, ECO:0007744|PDB:4KX9, ECO:0007744|PDB:4KXA, ECO:0007744|PDB:4KXB, ECO:0007744|PDB:4KXC, ECO:0007744|PDB:4KXD
ChainResidueDetails
AASN324
AASN763

site_idSWS_FT_FI12
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:23888046, ECO:0007744|PDB:4KX8, ECO:0007744|PDB:4KX9, ECO:0007744|PDB:4KXA, ECO:0007744|PDB:4KXB, ECO:0007744|PDB:4KXC
ChainResidueDetails
AASN340

site_idSWS_FT_FI13
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:23888046, ECO:0007744|PDB:4KX7, ECO:0007744|PDB:4KX8, ECO:0007744|PDB:4KX9, ECO:0007744|PDB:4KXA, ECO:0007744|PDB:4KXC, ECO:0007744|PDB:4KXD
ChainResidueDetails
AASN554

site_idSWS_FT_FI14
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN589

site_idSWS_FT_FI15
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:23888046, ECO:0007744|PDB:4KX8, ECO:0007744|PDB:4KXD
ChainResidueDetails
AASN597

site_idSWS_FT_FI16
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN607

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon