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6ENM

Crystal structure of MMP12 in complex with hydroxamate inhibitor LP168.

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 Residues19
Detailsbinding site for residue LPW A 301
ChainResidue
AGLY179
AHIS228
AVAL235
APHE237
APRO238
ATHR239
ATYR240
AZN302
AHOH517
BSER230
BPRO232
AILE180
ALEU181
AALA182
ALEU214
ATHR215
AHIS218
AGLU219
AHIS222

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 302
ChainResidue
AHIS218
AHIS222
AHIS228
ALPW301

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN A 303
ChainResidue
AHIS168
AASP170
AHIS183
AHIS196

site_idAC4
Number of Residues7
Detailsbinding site for residue CA A 304
ChainResidue
AASP158
AGLY190
AGLY192
AASP194
AHOH401
AHOH413
AHOH484

site_idAC5
Number of Residues5
Detailsbinding site for residue CA A 305
ChainResidue
AASP124
AGLU199
AGLU201
AHOH527
AHOH531

site_idAC6
Number of Residues6
Detailsbinding site for residue CA A 306
ChainResidue
AASP175
AGLY176
AGLY178
AILE180
AASP198
AGLU201

site_idAC7
Number of Residues18
Detailsbinding site for residue LPW B 301
ChainResidue
ASER230
BGLY179
BILE180
BLEU181
BALA182
BLEU214
BHIS218
BGLU219
BHIS222
BHIS228
BVAL235
BPHE237
BPRO238
BTHR239
BTYR240
BZN302
BHOH505
BHOH515

site_idAC8
Number of Residues4
Detailsbinding site for residue ZN B 302
ChainResidue
BHIS218
BHIS222
BHIS228
BLPW301

site_idAC9
Number of Residues4
Detailsbinding site for residue ZN B 303
ChainResidue
BHIS168
BASP170
BHIS183
BHIS196

site_idAD1
Number of Residues6
Detailsbinding site for residue CA B 304
ChainResidue
BASP158
BGLY190
BGLY192
BASP194
BHOH418
BHOH447

site_idAD2
Number of Residues5
Detailsbinding site for residue CA B 305
ChainResidue
BASP124
BGLU199
BGLU201
BHOH509
BHOH545

site_idAD3
Number of Residues6
Detailsbinding site for residue CA B 306
ChainResidue
BASP175
BGLY176
BGLY178
BILE180
BASP198
BGLU201

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 Residues2
DetailsActive site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues38
DetailsBinding site: {}
ChainResidueDetails

240971

PDB entries from 2025-08-27

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