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5UE3

proMMP-9desFnII

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 301
ChainResidue
ACYS99
AHIS226
AHIS230
AHIS236

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 Residues5
Detailsbinding site for residue CA A 304
ChainResidue
ASER129
AGLU130
AASP206
AHOH487
AHOH691

site_idAC5
Number of Residues6
Detailsbinding site for residue CA A 305
ChainResidue
AASP165
AGLY197
AGLN199
AASP201
AHOH412
AHOH485

site_idAC6
Number of Residues6
Detailsbinding site for residue SO4 A 306
ChainResidue
ATRP116
AHIS117
AHIS118
AHOH423
AHOH469
AHOH583

site_idAC7
Number of Residues8
Detailsbinding site for residue SO4 A 307
ChainResidue
AHIS118
AHIS118
AHIS119
AHIS119
AASN120
AASN120
AHOH512
AHOH512

site_idAC8
Number of Residues4
Detailsbinding site for residue ZN B 301
ChainResidue
BCYS99
BHIS226
BHIS230
BHIS236

site_idAC9
Number of Residues4
Detailsbinding site for residue ZN B 302
ChainResidue
BHIS175
BASP177
BHIS190
BHIS203

site_idAD1
Number of Residues6
Detailsbinding site for residue CA B 303
ChainResidue
BASP182
BGLY183
BASP185
BLEU187
BASP205
BGLU208

site_idAD2
Number of Residues6
Detailsbinding site for residue CA B 304
ChainResidue
BASP165
BGLY197
BGLN199
BASP201
BHOH443
BHOH463

site_idAD3
Number of Residues8
Detailsbinding site for residue SO4 B 305
ChainResidue
BTRP116
BHIS117
BHIS118
BHOH435
BHOH456
BHOH457
BHOH517
BHOH593

site_idAD4
Number of Residues10
Detailsbinding site for residue SO4 B 306
ChainResidue
AGLY105
AARG106
BSER211
BGLY215
BGLN216
BGLY217
BHOH493
BHOH501
BHOH522
BHOH563

site_idAD5
Number of Residues4
Detailsbinding site for residue SO4 B 307
ChainResidue
BASP103
BLEU104
BGLY105
BASP235

site_idAD6
Number of Residues8
Detailsbinding site for residue SO4 B 308
ChainResidue
BGLU241
BARG249
BTHR251
BHIS257
BHOH408
BHOH414
BHOH415
BHOH440

site_idAD7
Number of Residues11
Detailsbinding site for residue TRS B 309
ChainResidue
BHOH482
BLEU222
BVAL223
BHIS226
BLEU243
BMET247
BTYR248
BARG249
BHOH402
BHOH429
BHOH475

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

site_idPS00546
Number of Residues8
DetailsCYSTEINE_SWITCH Matrixins cysteine switch. PRCGvPDL
ChainResidueDetails
APRO97-LEU104

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:12051944
ChainResidueDetails
AGLU227
BGLU227

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: in inhibited form => ECO:0000269|PubMed:12051944, ECO:0000269|PubMed:12077439
ChainResidueDetails
ACYS99
BCYS99

site_idSWS_FT_FI3
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:12051944
ChainResidueDetails
AASP131
AASP205
AASP206
AGLU208
BASP131
BASP165
BASP182
BGLY183
BASP185
BLEU187
BGLY197
AASP165
BGLN199
BASP201
BASP205
BASP206
BGLU208
AASP182
AGLY183
AASP185
ALEU187
AGLY197
AGLN199
AASP201

site_idSWS_FT_FI4
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:12051944, ECO:0000269|PubMed:12077439
ChainResidueDetails
AHIS175
BHIS190
BHIS203
BHIS226
BHIS230
BHIS236
AASP177
AHIS190
AHIS203
AHIS226
AHIS230
AHIS236
BHIS175
BASP177

site_idSWS_FT_FI5
Number of Residues4
DetailsSITE: Cleavage; by MMP3 => ECO:0000269|PubMed:1371271
ChainResidueDetails
AGLU59
AARG106
BGLU59
BARG106

site_idSWS_FT_FI6
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN38
AASN120
AASN127
BASN38
BASN120
BASN127

223166

PDB entries from 2024-07-31

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