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3KEC

Crystal Structure of Human MMP-13 complexed with a phenyl-2H-tetrazole compound

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 Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 901
ChainResidue
AHIS222
AHIS226
AHIS232
AHAE272

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 902
ChainResidue
AHIS172
AASP174
AHIS187
AHIS200

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 903
ChainResidue
AGLY180
ASER182
ALEU184
AASP202
AGLU205
AASP179

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 904
ChainResidue
AHOH3
AHOH57
AASP162
AASN194
AGLY196
AASP198

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA A 905
ChainResidue
AASP128
AASP203
AGLU205

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1
ChainResidue
AHOH27
ALYS139
AARG155

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 2
ChainResidue
ALYS170
BSER182

site_idAC8
Number of Residues19
DetailsBINDING SITE FOR RESIDUE 3KE A 271
ChainResidue
ALYS140
AASN215
APHE217
ALEU218
AVAL219
AHIS222
AGLU223
AALA238
ALEU239
APHE241
APRO242
AILE243
ATYR244
ATHR245
ATHR247
ALYS249
ASER250
AHIS251
APHE252

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE HAE A 272
ChainResidue
ALEU184
AALA186
AHIS222
AGLU223
AHIS232
AHOH277
AZN901

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 901
ChainResidue
BHIS222
BHIS226
BHIS232
BHAE271

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 902
ChainResidue
BHIS172
BASP174
BHIS187
BHIS200

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 903
ChainResidue
BASP179
BGLY180
BSER182
BLEU184
BASP202
BGLU205

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 904
ChainResidue
BHOH22
BHOH46
BASP162
BASN194
BGLY196
BASP198

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 905
ChainResidue
BHOH45
BASP128
BASP203
BGLU205
BHOH277

site_idBC6
Number of Residues20
DetailsBINDING SITE FOR RESIDUE 3KE B 2
ChainResidue
BLYS140
BASN215
BPHE217
BLEU218
BVAL219
BHIS222
BGLU223
BALA238
BLEU239
BPHE241
BPRO242
BILE243
BTYR244
BTHR245
BTYR246
BTHR247
BLYS249
BPHE252
BHOH301
BHOH326

site_idBC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HAE B 271
ChainResidue
BHOH67
BALA186
BGLU223
BHIS226
BZN901

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VAAHEFGHSL
ChainResidueDetails
AVAL219-LEU228

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues140
DetailsRegion: {"description":"Interaction with TIMP2"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PubMed","id":"23913860","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues24
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_FI4
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_FI5
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"8576151","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

243531

PDB entries from 2025-10-22

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