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3F17

Crystal structure of the catalytic domain of human MMP12 complexed with the inhibitor N-(2-nitroso-2-oxoethyl)biphenyl-4-sulfonamide

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 264
ChainResidue
AHS40
AHIS218
AHIS222
AHIS228

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
AHOH66
AASP158
AGLY190
AGLY192
AASP194
AHOH12

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 267
ChainResidue
AHOH6
AHOH13
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 Residues16
DetailsBINDING SITE FOR RESIDUE HS4 A 0
ChainResidue
AHOH8
AGLY179
AILE180
ALEU181
AALA182
ALEU214
AHIS218
AGLU219
AHIS222
AHIS228
AVAL235
APHE237
APRO238
ATYR240
AZN264
AHOH415

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
AHIS168
AASP170
AASP175
AGLY176
AGLY178
AILE180
AHIS183
AGLY190
AGLY192
AASP194
AHIS196
AASP198
AGLU199
AGLU201
AHIS218
AHIS222
AHIS228
AASP158

221051

PDB entries from 2024-06-12

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