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5X49

Crystal Structure of Human mitochondrial X-prolyl Aminopeptidase (XPNPEP3)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003094biological_processglomerular filtration
A0004177molecular_functionaminopeptidase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0016485biological_processprotein processing
A0030145molecular_functionmanganese ion binding
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
A0070006molecular_functionmetalloaminopeptidase activity
B0003094biological_processglomerular filtration
B0004177molecular_functionaminopeptidase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0006508biological_processproteolysis
B0008237molecular_functionmetallopeptidase activity
B0016485biological_processprotein processing
B0030145molecular_functionmanganese ion binding
B0042803molecular_functionprotein homodimerization activity
B0046872molecular_functionmetal ion binding
B0070006molecular_functionmetalloaminopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue MN A 601
ChainResidue
AASP342
AHIS424
AGLU451
AGLU475
AMN602
A01B604

site_idAC2
Number of Residues6
Detailsbinding site for residue MN A 602
ChainResidue
AGLU475
AMN601
A01B604
AASP331
AASP342
ATHR344

site_idAC3
Number of Residues9
Detailsbinding site for residue 12P A 603
ChainResidue
ALYS78
ATYR123
AARG242
ALEU243
AILE246
ALEU440
AGLN443
ADMS606
AHOH926

site_idAC4
Number of Residues14
Detailsbinding site for residue 01B A 604
ChainResidue
ATYR300
APRO301
AHIS314
AASP331
AASP342
AHIS424
AHIS431
AGLU451
AGLU475
AMN601
AMN602
ADMS607
BILE111
BHOH858

site_idAC5
Number of Residues6
Detailsbinding site for residue DMS A 605
ChainResidue
ALEU313
AHIS420
AGLU451
AARG473
AHOH798
BTRP163

site_idAC6
Number of Residues4
Detailsbinding site for residue DMS A 606
ChainResidue
AGLU71
ALEU74
A12P603
AHOH779

site_idAC7
Number of Residues4
Detailsbinding site for residue DMS A 607
ChainResidue
AHIS421
AARG438
AGLU451
A01B604

site_idAC8
Number of Residues2
Detailsbinding site for residue EDO A 608
ChainResidue
ALEU298
BMET107

site_idAC9
Number of Residues6
Detailsbinding site for residue MN B 601
ChainResidue
BASP342
BHIS424
BGLU451
BGLU475
BMN602
B01B604

site_idAD1
Number of Residues6
Detailsbinding site for residue MN B 602
ChainResidue
BASP331
BASP342
BTHR344
BGLU475
BMN601
B01B604

site_idAD2
Number of Residues10
Detailsbinding site for residue 12P B 603
ChainResidue
BLYS78
BTYR123
BARG242
BLEU243
BILE246
BLEU440
BGLN443
BDMS606
BHOH763
BHOH895

site_idAD3
Number of Residues14
Detailsbinding site for residue 01B B 604
ChainResidue
AILE111
BTYR300
BPRO301
BHIS314
BASP331
BASP342
BHIS424
BHIS431
BGLU451
BGLU475
BMN601
BMN602
BDMS607
BHOH873

site_idAD4
Number of Residues6
Detailsbinding site for residue DMS B 605
ChainResidue
ATRP163
BLEU313
BHIS420
BGLU451
BARG473
BHOH880

site_idAD5
Number of Residues4
Detailsbinding site for residue DMS B 606
ChainResidue
BGLU71
BLEU74
B12P603
BHOH1093

site_idAD6
Number of Residues6
Detailsbinding site for residue DMS B 607
ChainResidue
BARG438
BGLU451
B01B604
BHOH925
AHOH1072
BHIS421

site_idAD7
Number of Residues2
Detailsbinding site for residue EDO B 608
ChainResidue
AHOH726
BLEU298

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:28476889, ECO:0007744|PDB:5X49
ChainResidueDetails
ATYR300
BGLU451
AASP331
AHIS424
AHIS431
AGLU451
BTYR300
BASP331
BHIS424
BHIS431

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:28476889, ECO:0000305|PubMed:25609706, ECO:0007744|PDB:5X49
ChainResidueDetails
AASP342
AGLU475
BASP342
BGLU475

227111

PDB entries from 2024-11-06

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