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1EUB

SOLUTION STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN COLLAGENASE-3 (MMP-13) COMPLEXED TO A POTENT NON-PEPTIDIC SULFONAMIDE INHIBITOR

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 Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 275
ChainResidue
AHIS172
AHIS187
AHIS200

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 276
ChainResidue
AHAV1
AHIS222
AHIS226
AHIS232
AMET240

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 277
ChainResidue
AASN194
ATYR195
AGLY196
AASP198
AASP162

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 278
ChainResidue
AASP179
AGLY180
APRO181
ASER182
ALEU184
AASP202
AGLU205

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE HAV A 1
ChainResidue
A3MP2
AMSB3
ALEU184
AALA186
AHIS222
AGLU223
AHIS226
AHIS232
AZN276

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE 3MP A 2
ChainResidue
AHAV1
AMSB3
AGLY183
APRO242

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE MSB A 3
ChainResidue
AHAV1
A3MP2
ALEU185
AALA186
ALEU218
AHIS222
APHE241
APRO242
AILE243
ATYR244

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 Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:23913860
ChainResidueDetails
AGLU223

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:10926524, ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645, ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980, ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229, ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512, ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497, ECO:0000269|PubMed:23913860, ECO:0000269|PubMed:8969305
ChainResidueDetails
AASP128
AASP202
AASP203
AGLU205
AASP162
AASP179
AGLY180
ASER182
ALEU184
AASN194
AGLY196
AASP198

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:10926524, ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645, ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980, ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229, ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512, ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497, ECO:0000269|PubMed:23913860
ChainResidueDetails
AHIS172
AASP174
AHIS187
AHIS200
AHIS222
AHIS226
AHIS232
AMET240

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:8576151
ChainResidueDetails
AASN117

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN152

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
AGLU223
AMET240

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
AGLU223

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PDB entries from 2024-07-24

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