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2JNP

Solution structure of matrix metalloproteinase 3 (MMP-3) in the presence of N-isobutyl-N-[4-methoxyphenylsulfonyl]glycyl hydroxamic acid (NNGH)

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 249
ChainResidue
AHIS151
AASP153
AHIS166
AHIS179

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 250
ChainResidue
AHIS201
AHIS205
AHIS211
ANGH253

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 251
ChainResidue
AGLY159
AGLY161
AVAL163
AASP181
AGLU184
AASP158

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 252
ChainResidue
AASP141
AGLY173
AASN175
AGLY176
AASP177

site_idAC5
Number of Residues14
DetailsBINDING SITE FOR RESIDUE NGH A 253
ChainResidue
AASN162
AVAL163
ALEU164
AALA165
AHIS166
AALA167
ALEU197
AHIS201
AGLU202
AHIS205
AHIS211
ALEU218
ATYR220
AZN250

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VAAHEIGHSL
ChainResidueDetails
AVAL198-LEU207

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE:
ChainResidueDetails
AGLU202

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING:
ChainResidueDetails
AASP107
AGLY173
AASN175
AASP177
AHIS179
AASP181
AASP182
AGLU184
AASP141
AHIS151
AASP153
AASP158
AGLY159
AGLY161
AVAL163
AHIS166

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:8740360
ChainResidueDetails
AHIS201
AHIS205
AHIS211

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
AMET219
AGLU202

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
AGLU202

site_idMCSA1
Number of Residues4
DetailsM-CSA 591
ChainResidueDetails
AHIS201metal ligand
AGLU202proton acceptor, proton donor
AHIS205metal ligand
AHIS211metal ligand

222415

PDB entries from 2024-07-10

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