Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5M4J

Crystal Structure of Wild-Type Human Prolidase with GlyPro ligand

Functional Information from GO Data
ChainGOidnamespacecontents
A0004181molecular_functionmetallocarboxypeptidase activity
A0005515molecular_functionprotein binding
A0006508biological_processproteolysis
A0006520biological_processamino acid metabolic process
A0008233molecular_functionpeptidase activity
A0008235molecular_functionmetalloexopeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0016787molecular_functionhydrolase activity
A0016805molecular_functiondipeptidase activity
A0030145molecular_functionmanganese ion binding
A0030574biological_processcollagen catabolic process
A0043069biological_processnegative regulation of programmed cell death
A0046872molecular_functionmetal ion binding
A0070006molecular_functionmetalloaminopeptidase activity
A0070062cellular_componentextracellular exosome
A0102009molecular_functionproline dipeptidase activity
A0140633biological_processCARD8 inflammasome complex assembly
B0004181molecular_functionmetallocarboxypeptidase activity
B0005515molecular_functionprotein binding
B0006508biological_processproteolysis
B0006520biological_processamino acid metabolic process
B0008233molecular_functionpeptidase activity
B0008235molecular_functionmetalloexopeptidase activity
B0008237molecular_functionmetallopeptidase activity
B0016787molecular_functionhydrolase activity
B0016805molecular_functiondipeptidase activity
B0030145molecular_functionmanganese ion binding
B0030574biological_processcollagen catabolic process
B0043069biological_processnegative regulation of programmed cell death
B0046872molecular_functionmetal ion binding
B0070006molecular_functionmetalloaminopeptidase activity
B0070062cellular_componentextracellular exosome
B0102009molecular_functionproline dipeptidase activity
B0140633biological_processCARD8 inflammasome complex assembly
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue NA A 499
ChainResidue
AASP287
AHIS370
AGLU412
AGLU452
ANA500
AGLY503

site_idAC2
Number of Residues7
Detailsbinding site for residue NA A 500
ChainResidue
AGLU452
ANA499
AGLY503
APRO504
AASP276
AASP287
AGLU412

site_idAC3
Number of Residues10
Detailsbinding site for residue GLY A 503
ChainResidue
ATYR241
AILE244
AASP276
AASP287
AHIS370
AHIS377
ANA499
ANA500
APRO504
AHOH768

site_idAC4
Number of Residues10
Detailsbinding site for residue PRO A 504
ChainResidue
ALEU254
AHIS255
AHIS377
AARG398
AGLU412
AARG450
ANA500
AGLY503
AHOH801
AHOH824

site_idAC5
Number of Residues8
Detailsbinding site for residue GOL A 505
ChainResidue
APHE9
ATRP10
ALEU11
ALYS120
AHOH602
AHOH611
AHOH626
BASP264

site_idAC6
Number of Residues6
Detailsbinding site for residue NA B 499
ChainResidue
BASP287
BHIS370
BGLU412
BGLU452
BNA500
BGLY503

site_idAC7
Number of Residues7
Detailsbinding site for residue NA B 500
ChainResidue
BASP276
BASP287
BGLU412
BGLU452
BNA499
BGLY503
BPRO504

site_idAC8
Number of Residues10
Detailsbinding site for residue GLY B 503
ChainResidue
BTYR241
BILE244
BASP276
BASP287
BHIS370
BHIS377
BNA499
BNA500
BPRO504
BHOH884

site_idAC9
Number of Residues11
Detailsbinding site for residue PRO B 504
ChainResidue
ATRP107
BLEU254
BHIS255
BHIS377
BARG398
BGLU412
BARG450
BNA500
BGLY503
BHOH734
BHOH801

site_idAD1
Number of Residues5
Detailsbinding site for residue GOL B 505
ChainResidue
BALA342
BHIS343
BLEU347
BSER348
BHOH783

site_idAD2
Number of Residues10
Detailsbinding site for residue GOL B 506
ChainResidue
AHIS255
AHIS377
AHOH1010
BASP60
BTHR61
BGLY62
BHOH621
BHOH643
BHOH674
BHOH984

site_idAD3
Number of Residues6
Detailsbinding site for residue GOL B 507
ChainResidue
AASP264
BPHE9
BTRP10
BHOH608
BHOH610
BHOH865

site_idAD4
Number of Residues2
Detailsbinding site for residue GOL B 508
ChainResidue
BGLU387
BARG388

Functional Information from PROSITE/UniProt
site_idPS00491
Number of Residues13
DetailsPROLINE_PEPTIDASE Aminopeptidase P and proline dipeptidase signature. HGLGHfLGIdVHD
ChainResidueDetails
AHIS366-ASP378

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"28677335","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5M4J","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5M4L","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"28677335","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5M4G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5M4L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5M4Q","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

PDB statisticsPDBj update infoContact PDBjnumon