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5M4Q

Crystal Structure of Wild-Type Human Prolidase with Mn ions and Pro 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
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
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue MN A 499
ChainResidue
AASP287
AHIS370
AGLU412
AGLU452
AMN500
AOH501
AHOH619

site_idAC2
Number of Residues7
Detailsbinding site for residue MN A 500
ChainResidue
ATHR289
AGLU452
AMN499
AOH501
AHOH877
AASP276
AASP287

site_idAC3
Number of Residues9
Detailsbinding site for residue OH A 501
ChainResidue
AASP276
AASP287
AGLU412
AGLU452
AMN499
AMN500
APRO504
AHOH619
AHOH877

site_idAC4
Number of Residues10
Detailsbinding site for residue PRO A 504
ChainResidue
AHIS255
AHIS366
AHIS377
AARG398
AGLU412
AOH501
AHOH619
AHOH702
AHOH734
BTRP107

site_idAC5
Number of Residues5
Detailsbinding site for residue GOL A 505
ChainResidue
APHE9
ATRP10
AHOH603
AHOH621
BASP264

site_idAC6
Number of Residues9
Detailsbinding site for residue GOL A 506
ChainResidue
AHIS330
AARG331
AASP334
AHIS358
AGLU391
APRO392
ALEU394
AHOH602
AHOH605

site_idAC7
Number of Residues4
Detailsbinding site for residue GOL A 507
ChainResidue
ATHR152
AGLU387
AARG388
AHOH715

site_idAC8
Number of Residues5
Detailsbinding site for residue GOL A 508
ChainResidue
AALA342
AHIS343
ALEU347
ASER348
AHOH676

site_idAC9
Number of Residues7
Detailsbinding site for residue MN B 499
ChainResidue
BASP287
BHIS370
BGLU412
BGLU452
BMN500
BOH501
BHOH631

site_idAD1
Number of Residues7
Detailsbinding site for residue MN B 500
ChainResidue
BASP276
BASP287
BTHR289
BGLU452
BMN499
BOH501
BHOH871

site_idAD2
Number of Residues9
Detailsbinding site for residue OH B 501
ChainResidue
BASP276
BASP287
BGLU412
BGLU452
BMN499
BMN500
BPRO504
BHOH631
BHOH871

site_idAD3
Number of Residues10
Detailsbinding site for residue PRO B 504
ChainResidue
ATRP107
BHIS255
BHIS366
BHIS377
BARG398
BGLU412
BOH501
BHOH631
BHOH754
BHOH800

site_idAD4
Number of Residues9
Detailsbinding site for residue GOL B 505
ChainResidue
AASP264
BPHE9
BTRP10
BLEU11
BLYS120
BHOH674
BHOH752
BHOH757
BHOH965

site_idAD5
Number of Residues5
Detailsbinding site for residue GOL B 506
ChainResidue
BGLY165
BILE166
BSER167
BHOH662
BASP164

site_idAD6
Number of Residues10
Detailsbinding site for residue GOL B 507
ChainResidue
AGLU227
AHIS228
ATYR231
AHOH895
BSER224
BGLU227
BHIS228
BHOH632
BHOH819
BHOH834

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

246905

PDB entries from 2025-12-31

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