Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2WI0

Dipeptide Inhibitors of Thermolysin

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1317
ChainResidue
AHIS142
AHIS146
AGLU166
AHOH2326

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1318
ChainResidue
AHOH2216
AASP138
AGLU177
AASP185
AGLU187
AGLU190

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1319
ChainResidue
AGLU177
AASN183
AASP185
AGLU190
AHOH2220
AHOH2221

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1320
ChainResidue
AASP57
AASP59
AGLN61
AHOH2100
AHOH2103
AHOH2119

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1321
ChainResidue
ATYR193
ATHR194
AILE197
AASP200
AHOH2219
AHOH2226

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE LEU A 1001
ChainResidue
AASN112
AALA113
AGLU143
ALEU202
AARG203
AHIS231
ATRP1002
AHOH2326

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE TRP A 1002
ChainResidue
AASN111
AASN112
APHE130
ALEU202
AHIS231
ALEU1001
APEG1324
AHOH2327

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PEG A 1324
ChainResidue
AGLY109
ATYR110
AASN111
AASN112
AGLN158
AASN227
ATRP1002

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_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

245663

PDB entries from 2025-12-03

PDB statisticsPDBj update infoContact PDBjnumon