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5D2B

Crystal structure of a mutated catalytic domain of Human MMP12 in complex with an hydroxamate analogue of RXP470

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 301
ChainResidue
AHIS218
AHIS222
AHIS228
A56O306

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 302
ChainResidue
AHIS168
AASP170
AHIS183
AHIS196

site_idAC3
Number of Residues6
Detailsbinding site for residue CA A 303
ChainResidue
AGLY190
AGLY192
AASP194
AHOH441
AHOH456
AASP158

site_idAC4
Number of Residues5
Detailsbinding site for residue CA A 304
ChainResidue
AASP124
AGLU199
AGLU201
AHOH552
AHOH588

site_idAC5
Number of Residues6
Detailsbinding site for residue CA A 305
ChainResidue
AASP175
AGLY176
AGLY178
AILE180
AASP198
AGLU201

site_idAC6
Number of Residues34
Detailsbinding site for residue 56O A 306
ChainResidue
ATHR154
AGLY155
AGLY178
AGLY179
AILE180
ALEU181
AALA182
ATHR215
AHIS218
AGLU219
AHIS222
AHIS228
APRO232
APRO232
ALYS233
AALA234
AVAL235
APHE237
APRO238
ATHR239
ATYR240
ALYS241
AVAL243
APHE248
AZN301
AHOH401
AHOH404
AHOH406
AHOH407
AHOH411
AHOH416
AHOH422
AHOH424
AHOH578

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

222036

PDB entries from 2024-07-03

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