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7TLN

STRUCTURAL ANALYSIS OF THE INHIBITION OF THERMOLYSIN BY AN ACTIVE-SITE-DIRECTED IRREVERSIBLE INHIBITOR

Replaces:  6TLN
Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 317
ChainResidue
AASP138
AGLU177
AASP185
AGLU187
AGLU190
ACA318
AHOH346

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 318
ChainResidue
AASP185
AGLU190
ACA317
AHOH353
AHOH475
AGLU177
AASN183

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 319
ChainResidue
AASP57
AASP59
AGLN61
AHOH419
AHOH482
AHOH503

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 320
ChainResidue
ATYR193
ATHR194
AILE197
AASP200
AHOH354
AHOH480

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 321
ChainResidue
AHIS142
AHIS146
AGLU166
AINC322

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE INC A 322
ChainResidue
AASN112
AALA113
AGLU143
AHIS146
ATYR157
AGLU166
AARG203
AHIS231
AZN321
AHOH362

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

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PDB entries from 2025-12-24

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