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1Y93

Crystal structure of the catalytic domain of human MMP12 complexed with acetohydroxamic acid at atomic resolution

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 Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 264
ChainResidue
AHIS218
AHIS222
AHIS228
AHAE301
AHOH408

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
AASP158
AGLY190
AGLY192
AASP194
AHOH308
AHOH346

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 267
ChainResidue
AASP124
AGLU199
AGLU201
AHOH310
AHOH319

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 268
ChainResidue
AASP175
AGLY176
AGLY178
AILE180
AASP198
AGLU201

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE HAE A 301
ChainResidue
AALA182
AHIS218
AGLU219
AHIS222
AHIS228
AZN264
AHOH328
AHOH408
AHOH450

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

218853

PDB entries from 2024-04-24

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