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4FU4

Human collagenase 3 (MMP-13) with peptide from pro-domain

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0031012cellular_componentextracellular matrix
B0004222molecular_functionmetalloendopeptidase activity
B0006508biological_processproteolysis
B0008237molecular_functionmetallopeptidase activity
B0008270molecular_functionzinc ion binding
B0031012cellular_componentextracellular matrix
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 501
ChainResidue
AHIS222
AHIS226
AHIS232
CALA39
CGLU40
CCL101

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 502
ChainResidue
AHIS200
AHIS172
AASP174
AHIS187

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 503
ChainResidue
AASP179
AGLY180
ASER182
ALEU184
AASP202
AGLU205

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 504
ChainResidue
AASP162
AASN194
AGLY196
AASP198

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 505
ChainResidue
AASP291
AASP335
ASER383
AASP432
AHOH610

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 506
ChainResidue
AILE293
AALA337
AALA385
AVAL434
ACL507

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 507
ChainResidue
AILE293
AALA337
AALA385
AVAL434
ACA506

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO A 508
ChainResidue
ASER467

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 509
ChainResidue
ATYR440
AGLU451
AARG461
CARG44

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 510
ChainResidue
ATYR416
AASP423
AEDO514

site_idBC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO A 511
ChainResidue
AHOH609

site_idBC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 512
ChainResidue
AASN194
ATYR195

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 513
ChainResidue
ATHR247
AMET253
AARG306

site_idBC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO A 514
ChainResidue
AEDO510

site_idBC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 515
ChainResidue
ATYR440
ATRP455

site_idBC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 516
ChainResidue
ATYR104
AASN105
AHOH626

site_idBC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 517
ChainResidue
AGLN263
ASER264

site_idBC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 518
ChainResidue
ALYS234
AASP317

site_idCC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 501
ChainResidue
BHIS222
BHIS226
BHIS232
DSER45
DCL101

site_idCC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 502
ChainResidue
BHIS172
BASP174
BHIS187
BHIS200

site_idCC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 503
ChainResidue
BASP179
BGLY180
BSER182
BLEU184
BASP202
BGLU205

site_idCC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA B 504
ChainResidue
BASP162
BASN194
BGLY196
BASP198

site_idCC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 505
ChainResidue
BASP291
BASP335
BSER383
BASP432
BHOH636
BHOH653

site_idCC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 506
ChainResidue
BILE293
BALA337
BALA385
BVAL434
BCL507
BHOH635

site_idCC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL B 507
ChainResidue
BALA292
BILE293
BALA337
BALA433
BVAL434
BCA506

site_idCC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO B 508
ChainResidue
BPHE326
BGLY359

site_idCC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 509
ChainResidue
BASP203
BASP204
BGLU205
BTHR206
BASP128

site_idDC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 510
ChainResidue
BTHR247
BPHE252
BMET253
BPRO255

site_idDC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 511
ChainResidue
APRO464
BASN445
BILE448

site_idDC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 512
ChainResidue
BPRO236
BTHR280
BPRO281
BHOH645

site_idDC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 513
ChainResidue
BTHR391
BLYS393
BILE454

site_idDC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO B 514
ChainResidue
BTYR104

site_idDC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO B 515
ChainResidue
BGLN260
BSER264

site_idDC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO B 516
ChainResidue
BGLN263
BGLY267

site_idDC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 517
ChainResidue
BGLY248
BLYS249
BSER250
BHIS251
BPHE252

site_idDC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 518
ChainResidue
BLYS437
BTYR442
BGLN449
BEDO519

site_idEC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 519
ChainResidue
BTRP470
BEDO518
DTYR47

site_idEC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO B 520
ChainResidue
BSER146
BTHR149
BPRO150
BLEU151
BASN152
BGLY269
BASP270
BHOH641

site_idEC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CL C 101
ChainResidue
AALA186
AHIS187
AHIS226
AZN501
CPHE38
CALA39
CGLU40

site_idEC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO C 102
ChainResidue
AARG297
CPRO49

site_idEC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL D 101
ChainResidue
BHIS222
BHIS226
BZN501
DARG44
DSER45
DTYR46

site_idEC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO D 102
ChainResidue
BHIS232
DARG44
DSER45
DTYR47

Functional Information from PROSITE/UniProt
site_idPS00024
Number of Residues16
DetailsHEMOPEXIN Hemopexin domain signature. TKsfWpelPnRIDAAY
ChainResidueDetails
ATHR323-TYR338

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues98
DetailsRepeat: {"description":"Hemopexin 1"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues92
DetailsRepeat: {"description":"Hemopexin 2"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues96
DetailsRepeat: {"description":"Hemopexin 3"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues86
DetailsRepeat: {"description":"Hemopexin 4"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues140
DetailsRegion: {"description":"Interaction with TIMP2"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues42
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues406
DetailsRegion: {"description":"Interaction with collagen"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues22
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PubMed","id":"23913860","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues40
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10926524","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10986126","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15734645","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15780611","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17196980","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17623656","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19422229","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20005097","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20726512","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22689580","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23810497","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23913860","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8969305","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10926524","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10986126","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15734645","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15780611","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17196980","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17623656","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19422229","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20005097","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20726512","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22689580","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23810497","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23913860","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine; by PKDCC","evidences":[{"source":"PubMed","id":"25171405","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"8576151","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

249697

PDB entries from 2026-02-25

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