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2TLX

THERMOLYSIN (NATIVE)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE VAL A 317
ChainResidue
AASN112
AALA113
AGLU143
AARG203
AHIS231
ALYS318
AHOH328
AHOH533

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE LYS A 318
ChainResidue
AASN112
APHE130
AHIS231
AVAL317
AHOH532
AASN111

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 322
ChainResidue
AHIS142
AHIS146
AGLU166
AHOH327
AHOH328

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 323
ChainResidue
AASP138
AGLU177
AASP185
AGLU187
AGLU190
AHOH340

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 324
ChainResidue
AGLU177
AASN183
AASP185
AGLU190
AHOH339
AHOH356

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 325
ChainResidue
AASP57
AASP59
AGLN61
AHOH342
AHOH353
AHOH373

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 326
ChainResidue
ATYR193
ATHR194
AILE197
AASP200
AHOH364
AHOH391

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE DMS A 321
ChainResidue
AHIS216
ASER218

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VVAHELTHAV
ChainResidueDetails
AVAL139-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_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1tlp
ChainResidueDetails
AHIS231
AGLU143

site_idMCSA1
Number of Residues7
DetailsM-CSA 176
ChainResidueDetails
AHIS142metal ligand
AGLU143electrostatic stabiliser, metal ligand
AHIS146metal ligand
ATYR157electrostatic stabiliser, hydrogen bond donor, steric role
AGLU166metal ligand
AASP226activator, electrostatic stabiliser, hydrogen bond acceptor
AHIS231hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

246031

PDB entries from 2025-12-10

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