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3T2I

Tetragonal thermolysin in the presence of sarcosine

Functional Information from GO Data
ChainGOidnamespacecontents
E0004222molecular_functionmetalloendopeptidase activity
E0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA E 317
ChainResidue
EASP138
EGLU177
EASP185
EGLU187
EGLU190
ECA318
EHOH414

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA E 318
ChainResidue
EASP185
EGLU190
ECA317
EHOH421
EHOH457
EGLU177
EASN183

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA E 319
ChainResidue
EASP57
EASP59
EGLN61
EHOH447
EHOH463
EHOH467

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA E 320
ChainResidue
ETYR193
ETHR194
EILE197
EASP200
EHOH422
EHOH462

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN E 321
ChainResidue
EHIS142
EHIS146
EGLU166
ECL324

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN E 322
ChainResidue
EHIS250
EHOH401
EHOH402
EHOH403

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL E 323
ChainResidue
EGLY12
ELEU14
EGLY15
EASP16
ELYS18

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CL E 324
ChainResidue
EHIS142
EGLU143
EHIS146
ETYR157
EGLU166
EHIS231
EZN321
EHOH499

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL E 325
ChainResidue
EARG285
EHOH517

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA E 326
ChainResidue
ETYR211
EHOH472
EHOH503
EHOH518
EHOH519
EHOH572

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SAR E 2001
ChainResidue
EALA209
ELYS210
ETYR211
EGLY212
EHOH519

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SAR E 2002
ChainResidue
EASN19
EASN21
EARG35
EHOH419
EHOH456

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SAR E 2003
ChainResidue
ETYR179
EALA180
EASN181
EARG269
EHOH584

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DMS E 2011
ChainResidue
ETYR66
EHIS216
EHOH543
EHOH578

site_idBC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE DMS E 2012
ChainResidue
ESER206
ETYR242

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VVAHELTHAV
ChainResidueDetails
EVAL139-VAL148

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"4808703","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"4808703","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 176
ChainResidueDetails

246704

PDB entries from 2025-12-24

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