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1CXV

STRUCTURE OF RECOMBINANT MOUSE COLLAGENASE-3 (MMP-13)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0031012cellular_componentextracellular matrix
B0004222molecular_functionmetalloendopeptidase activity
B0006508biological_processproteolysis
B0008237molecular_functionmetallopeptidase activity
B0008270molecular_functionzinc ion binding
B0031012cellular_componentextracellular matrix
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1
ChainResidue
ACBP10
AHIS201
AHIS205
AHIS211

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 2
ChainResidue
BCBP11
BHIS501
BHIS505
BHIS511

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 3
ChainResidue
AASP153
AHIS166
AHIS179
AHIS151

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 4
ChainResidue
BHIS451
BASP453
BHIS466
BHIS479

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 5
ChainResidue
ATRP92
AASP141
AGLY171
AASN173
AGLY175
AHOH665

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 6
ChainResidue
BASP441
BASN473
BGLY475
BASP477
BHOH664

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 7
ChainResidue
AASP158
AGLY159
ASER161
ALEU163
AASP181
AGLU184

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 8
ChainResidue
BASP458
BGLY459
BSER461
BLEU463
BASP481
BGLU484

site_idAC9
Number of Residues19
DetailsBINDING SITE FOR RESIDUE CBP A 10
ChainResidue
AZN1
ATYR155
ALEU163
ALEU164
AALA165
AILE197
AHIS201
AGLU202
AHIS205
AHIS211
ALEU218
APHE220
APRO221
AILE222
ATYR223
ATHR224
AHOH604
AHOH773
AHOH849

site_idBC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE CBP B 11
ChainResidue
BZN2
BLEU463
BLEU464
BALA465
BILE497
BHIS501
BGLU502
BHIS505
BHIS511
BLEU518
BPHE520
BPRO521
BILE522
BTYR523
BTHR524
BHOH738
BHOH759

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VAAHELGHSL
ChainResidueDetails
AVAL198-LEU207

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE:
ChainResidueDetails
AGLU202
BGLU502

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASP107
BMET519
AASN173
AASP177
AASP182
AMET219
BASP407
BASN473
BASP477
BASP482

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING:
ChainResidueDetails
AASP141
BASP458
BGLY459
BSER461
BLEU463
BGLY475
BASP481
BGLU484
AASP158
AGLY159
ASER161
ALEU163
AGLY175
AASP181
AGLU184
BASP441

site_idSWS_FT_FI4
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:10525409
ChainResidueDetails
AHIS151
BHIS466
BHIS479
BHIS501
BHIS505
BHIS511
AASP153
AHIS166
AHIS179
AHIS201
AHIS205
AHIS211
BHIS451
BASP453

site_idSWS_FT_FI5
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN96
AASN131
BASN396
BASN431

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
AMET219
AGLU202

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
BMET519
BGLU502

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
AGLU202

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
BGLU502

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PDB entries from 2024-09-11

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