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3BA0

Crystal structure of full-length human MMP-12

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 471
ChainResidue
AHIS218
AGLU219
AHIS222
AHIS228

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 472
ChainResidue
AHIS168
AASP170
AHIS183
AHIS196

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA A 473
ChainResidue
AGLY192
AASP194
AASP158

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA A 474
ChainResidue
AASP124
AGLU199
AGLU201

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 475
ChainResidue
AASP175
AGLY176
AGLY178
AILE180
AASP198
AGLU201

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 476
ChainResidue
AASP289
AGLU333
AASP381
AASP430

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE HAE A 477
ChainResidue
AALA182
AGLU219
AHIS222

Functional Information from PROSITE/UniProt
site_idPS00024
Number of Residues16
DetailsHEMOPEXIN Hemopexin domain signature. ISslWptlPsGIEAAY
ChainResidueDetails
AILE321-TYR336

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

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASP289
AGLU333
AASP381
AASP430

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN285

218853

PDB entries from 2024-04-24

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