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5MC0

Crystal Structure of delTyr231 mutant of Human Prolidase with Mn ions and GlyPro ligand

Functional Information from GO Data
ChainGOidnamespacecontents
A0004181molecular_functionmetallocarboxypeptidase activity
A0005515molecular_functionprotein binding
A0006508biological_processproteolysis
A0006520biological_processamino acid metabolic process
A0008233molecular_functionpeptidase activity
A0008237molecular_functionmetallopeptidase 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
B0008237molecular_functionmetallopeptidase 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
AASP286
AHIS369
AGLU411
AGLU451
AMN500
AOH501
AGLY503

site_idAC2
Number of Residues7
Detailsbinding site for residue MN A 500
ChainResidue
ATHR288
AGLU451
AMN499
AOH501
AGLY503
AASP275
AASP286

site_idAC3
Number of Residues8
Detailsbinding site for residue OH A 501
ChainResidue
AASP275
AASP286
AGLU411
AGLU451
AMN499
AMN500
AGLY503
APRO504

site_idAC4
Number of Residues10
Detailsbinding site for residue GLY A 503
ChainResidue
ATYR240
AASP275
AASP286
AHIS369
AHIS376
AMN499
AMN500
AOH501
APRO504
AHOH648

site_idAC5
Number of Residues11
Detailsbinding site for residue PRO A 504
ChainResidue
AHIS254
AHIS365
AHIS376
AARG397
AGLU411
AARG449
AOH501
AGLY503
AHOH764
AHOH824
BTRP107

site_idAC6
Number of Residues8
Detailsbinding site for residue GOL A 506
ChainResidue
ATRP10
ALEU11
ALYS120
AHOH609
AHOH619
AHOH720
AHOH828
BASP263

site_idAC7
Number of Residues4
Detailsbinding site for residue GOL A 507
ChainResidue
ATHR152
AGLU386
AARG387
AHOH921

site_idAC8
Number of Residues4
Detailsbinding site for residue GOL A 508
ChainResidue
AGLY384
AGLU386
AALA399
AHOH655

site_idAC9
Number of Residues7
Detailsbinding site for residue GOL A 509
ChainResidue
AARG29
AARG33
ALYS36
AGLU182
APHE186
AHOH607
AHOH1016

site_idAD1
Number of Residues5
Detailsbinding site for residue GOL A 510
ChainResidue
APRO141
ALYS168
APHE169
AHOH836
AHOH851

site_idAD2
Number of Residues6
Detailsbinding site for residue NA A 511
ChainResidue
AGLY317
AHOH700
AHOH708
AHOH1036
AHOH1144
BALA39

site_idAD3
Number of Residues7
Detailsbinding site for residue MN B 499
ChainResidue
BASP286
BHIS369
BGLU411
BGLU451
BMN500
BOH501
BGLY503

site_idAD4
Number of Residues7
Detailsbinding site for residue MN B 500
ChainResidue
BASP275
BASP286
BTHR288
BGLU451
BMN499
BOH501
BGLY503

site_idAD5
Number of Residues8
Detailsbinding site for residue OH B 501
ChainResidue
BASP275
BASP286
BGLU411
BGLU451
BMN499
BMN500
BGLY503
BPRO504

site_idAD6
Number of Residues10
Detailsbinding site for residue GLY B 503
ChainResidue
BTYR240
BASP275
BASP286
BHIS369
BHIS376
BMN499
BMN500
BOH501
BPRO504
BHOH778

site_idAD7
Number of Residues10
Detailsbinding site for residue PRO B 504
ChainResidue
BHIS254
BHIS365
BHIS376
BARG397
BGLU411
BARG449
BOH501
BGLY503
BHOH743
BHOH900

site_idAD8
Number of Residues3
Detailsbinding site for residue CL B 506
ChainResidue
BARG436
BGLN440
BARG443

site_idAD9
Number of Residues8
Detailsbinding site for residue GOL B 507
ChainResidue
AASP263
BPHE9
BTRP10
BLEU11
BHOH622
BHOH645
BHOH722
BHOH785

site_idAE1
Number of Residues5
Detailsbinding site for residue GOL B 508
ChainResidue
BGLU14
BTYR197
BLYS200
BHOH637
BHOH641

site_idAE2
Number of Residues6
Detailsbinding site for residue GOL B 509
ChainResidue
BSER134
BSER138
BGLY348
BSER349
BVAL350
BASP351

site_idAE3
Number of Residues4
Detailsbinding site for residue GOL B 510
ChainResidue
BGLU386
BARG387
BHOH834
BHOH848

site_idAE4
Number of Residues6
Detailsbinding site for residue GOL B 511
ChainResidue
BPHE163
BASP164
BGLY165
BILE166
BSER167
BHOH625

site_idAE5
Number of Residues6
Detailsbinding site for residue GOL B 512
ChainResidue
BTYR83
BVAL129
BPHE163
BASP164
BHOH617
BHOH991

site_idAE6
Number of Residues4
Detailsbinding site for residue GOL B 513
ChainResidue
BLYS168
BHOH602
BHOH609
BHOH614

site_idAE7
Number of Residues2
Detailsbinding site for residue GOL B 514
ChainResidue
AHIS228
BHIS228

site_idAE8
Number of Residues7
Detailsbinding site for residue NA B 515
ChainResidue
BMET210
BLYS211
BVAL213
BMET478
BHOH611
BHOH1057
BHOH1100

Functional Information from PROSITE/UniProt
site_idPS00491
Number of Residues13
DetailsPROLINE_PEPTIDASE Aminopeptidase P and proline dipeptidase signature. HGLGHfLGIdVHD
ChainResidueDetails
AHIS365-ASP377

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:28677335, ECO:0007744|PDB:5M4J, ECO:0007744|PDB:5M4L
ChainResidueDetails
ATYR255
AASP377
ATHR398
BTYR255
BASP377
BTHR398

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:28677335, ECO:0007744|PDB:5M4G, ECO:0007744|PDB:5M4L, ECO:0007744|PDB:5M4Q
ChainResidueDetails
AMET276
BGLU452
AILE287
APHE370
APRO412
AGLU452
BMET276
BILE287
BPHE370
BPRO412

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER167
BSER167

224004

PDB entries from 2024-08-21

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