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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
DetailsACT_SITE:
ChainResidueDetails
AGLU219
BGLU219

site_idSWS_FT_FI2
Number of Residues38
DetailsBINDING:
ChainResidueDetails
AASP175
AGLY176
AGLY178
AILE180
AHIS183
AGLY190
AGLY192
AASP194
AHIS196
AASP198
AGLU199
AGLU201
AHIS218
AHIS222
AHIS228
BASP124
BASP158
BHIS168
BASP170
BASP175
BGLY176
BGLY178
BILE180
BHIS183
BGLY190
BGLY192
BASP194
BHIS196
BASP198
BGLU199
BGLU201
BHIS218
BHIS222
BHIS228
AASP124
AASP158
AHIS168
AASP170

221051

PDB entries from 2024-06-12

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