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5LAB

Crystal structure of the catalytic domain of human MMP12 complexed with the inhibitor NNGH

Replaces:  1RMZ
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
ANGH306

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
AHOH413
AHOH452
AASP158

site_idAC4
Number of Residues5
Detailsbinding site for residue CA A 304
ChainResidue
AASP124
AGLU199
AGLU201
AHOH525
AHOH541

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

site_idAC6
Number of Residues14
Detailsbinding site for residue NGH A 306
ChainResidue
AILE180
ALEU181
AALA182
AHIS218
AGLU219
AHIS222
AHIS228
ASER230
APRO238
ATYR240
AZN301
AHOH455
AHOH485
AHOH587

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
AHIS168
AASP170
AASP175
AGLY176
AGLY178
AILE180
AHIS183
AGLY190
AGLY192
AASP194
AHIS196
AASP198
AGLU199
AGLU201
AHIS218
AHIS222
AHIS228
AASP124
AASP158

220472

PDB entries from 2024-05-29

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