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2K2G

Solution structure of the wild-type catalytic domain of human matrix metalloproteinase 12 (MMP-12) in complex with a tight-binding 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 Residues2
DetailsBINDING SITE FOR RESIDUE ZN A 2
ChainResidue
AHIS218
AHIS222

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN A 3
ChainResidue
AHIS168
APHE171

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE DSV A 1
ChainResidue
AASN211
ALEU214
ATHR215
AHIS218
AHIS222
AHIS228
AMET236
AGLY179
AILE180
ALEU181
AHIS183
AALA184

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TAVHEIGHSL
ChainResidueDetails
ATHR215-LEU224

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE:
ChainResidueDetails
AGLU219

site_idSWS_FT_FI2
Number of Residues19
DetailsBINDING:
ChainResidueDetails
AASP124
AGLY190
AGLY192
AASP194
AHIS196
AASP198
AGLU199
AGLU201
AHIS218
AHIS222
AHIS228
AASP158
AHIS168
AASP170
AASP175
AGLY176
AGLY178
AILE180
AHIS183

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
AMET236
AGLU219

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
AGLU219

223532

PDB entries from 2024-08-07

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