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

4WZ9

APN1 from Anopheles gambiae

Functional Information from GO Data
ChainGOidnamespacecontents
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005886cellular_componentplasma membrane
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0016020cellular_componentmembrane
A0042277molecular_functionpeptide binding
A0042802molecular_functionidentical protein binding
A0043171biological_processpeptide catabolic process
A0046872molecular_functionmetal ion binding
A0070006molecular_functionmetalloaminopeptidase activity
A0098552cellular_componentside of membrane
B0005615cellular_componentextracellular space
B0005737cellular_componentcytoplasm
B0005886cellular_componentplasma membrane
B0006508biological_processproteolysis
B0008237molecular_functionmetallopeptidase activity
B0008270molecular_functionzinc ion binding
B0016020cellular_componentmembrane
B0042277molecular_functionpeptide binding
B0042802molecular_functionidentical protein binding
B0043171biological_processpeptide catabolic process
B0046872molecular_functionmetal ion binding
B0070006molecular_functionmetalloaminopeptidase activity
B0098552cellular_componentside of membrane
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 1001
ChainResidue
AHIS366
AHIS370
AGLU389
MALA1

site_idAC2
Number of Residues2
Detailsbinding site for residue GOL A 1002
ChainResidue
AASP701
ATHR741

site_idAC3
Number of Residues4
Detailsbinding site for residue GOL A 1003
ChainResidue
ATHR821
APHE783
AGLN784
AALA817

site_idAC4
Number of Residues8
Detailsbinding site for residue NHE A 1004
ChainResidue
AASP186
AARG191
AGLN271
APRO284
AASN285
APHE287
AASN896
AALA900

site_idAC5
Number of Residues4
Detailsbinding site for residue ZN B 1001
ChainResidue
BHIS366
BHIS370
BGLU389
NALA0

site_idAC6
Number of Residues4
Detailsbinding site for residue GOL B 1002
ChainResidue
BTHR173
BASP175
BVAL180
BASP326

site_idAC7
Number of Residues3
Detailsbinding site for residue GOL B 1003
ChainResidue
BGLN784
BARG788
BGLU830

site_idAC8
Number of Residues3
Detailsbinding site for residue GOL B 1004
ChainResidue
BGLU669
BTYR670
BHIS724

site_idAC9
Number of Residues3
Detailsbinding site for residue CU B 1005
ChainResidue
BGLU86
BARG87
BARG170

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TIAHEYAHQW
ChainResidueDetails
ATHR363-TRP372

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10095
ChainResidueDetails
AGLU367
BGLU367

site_idSWS_FT_FI2
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:26075520, ECO:0007744|PDB:4WZ9
ChainResidueDetails
AGLU199
BALA331
BGLU333
BHIS366
BHIS370
BGLU389
AGLY330
AALA331
AGLU333
AHIS366
AHIS370
AGLU389
BGLU199
BGLY330

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000305|PubMed:26075520
ChainResidueDetails
ATYR452
BTYR452

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon