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5I12

Crystal structure of the catalytic domain of MMP-9 in complex with a selective sugar-conjugated arylsulfonamide carboxylate water-soluble inhibitor (DC27).

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0031012cellular_componentextracellular matrix
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 301
ChainResidue
AHIS226
AHIS230
AHIS236
AH27306

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 302
ChainResidue
AHIS175
AASP177
AHIS190
AHIS203

site_idAC3
Number of Residues6
Detailsbinding site for residue CA A 303
ChainResidue
AGLY183
AASP185
ALEU187
AASP205
AGLU208
AASP182

site_idAC4
Number of Residues6
Detailsbinding site for residue CA A 304
ChainResidue
AASP165
AGLY197
AGLN199
AASP201
AHOH420
AHOH424

site_idAC5
Number of Residues5
Detailsbinding site for residue CA A 305
ChainResidue
AASP131
AASP206
AGLU208
AHOH451
AHOH476

site_idAC6
Number of Residues18
Detailsbinding site for residue H27 A 306
ChainResidue
ALEU187
ALEU188
AALA189
ALYS214
ALEU222
AHIS226
AGLU227
AHIS230
AHIS236
ALEU243
ATYR245
APRO246
AMET247
AASN262
AHIS266
AZN301
AGOL309
AHOH404

site_idAC7
Number of Residues5
Detailsbinding site for residue EDO A 307
ChainResidue
AASP113
ALYS115
ATRP116
AHIS117
AHIS118

site_idAC8
Number of Residues2
Detailsbinding site for residue DMS A 308
ChainResidue
ATYR179
AALA191

site_idAC9
Number of Residues6
Detailsbinding site for residue GOL A 309
ChainResidue
APRO240
AGLU241
AALA242
AARG249
ATHR251
AH27306

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VAAHEFGHAL
ChainResidueDetails
AVAL223-LEU232

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PubMed","id":"12051944","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12051944","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12051944","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12077439","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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