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3LKA

Catalytic domain of human MMP-12 complexed with hydroxamic acid and paramethoxy-sulfonyl amide

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 Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 264
ChainResidue
AHIS218
AHIS222
AHIS228
AHAE269
AHOH305

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 265
ChainResidue
AHIS168
AASP170
AHIS183
AHIS196

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 266
ChainResidue
AHOH7
AASP158
AGLY190
AGLY192
AASP194
AHOH289

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 267
ChainResidue
AHOH16
AHOH21
AASP124
AGLU199
AGLU201

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 268
ChainResidue
AASP175
AGLY176
AGLY178
AILE180
AASP198
AGLU201

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE HAE A 269
ChainResidue
AHOH10
AHOH97
AALA182
AHIS183
AHIS218
AGLU219
AHIS222
AHIS228
AZN264
AHOH305

site_idAC7
Number of Residues11
DetailsBINDING SITE FOR RESIDUE M4S A 1
ChainResidue
AHOH64
ALEU181
AALA182
ALEU214
ATHR215
AHIS218
AGLU219
APRO238
ATYR240
AHOH285
AHOH305

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

229183

PDB entries from 2024-12-18

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