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5FSS

Structure of thermolysin prepared by the 'soak-and-freeze' method under 40 bar of krypton pressure

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 401
ChainResidue
AASP138
AGLU177
AASP185
AGLU187
AGLU190
AHOH2217

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 402
ChainResidue
AGLU190
AHOH2220
AHOH2223
AGLU177
AASN183
AASP185

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 403
ChainResidue
AASP57
AASP59
AGLN61
AHOH2109
AHOH2110
AHOH2112

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 404
ChainResidue
ATYR193
ATHR194
AILE197
AASP200
AHOH2228
AHOH2231

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 405
ChainResidue
AHIS142
AHIS146
AGLU166
AZN406

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 406
ChainResidue
AHIS142
ATYR157
AGLU166
AHIS231
AZN405
AVAL1001

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE KR A 407
ChainResidue
ATYR84
ASER92
ATYR93

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE KR A 408
ChainResidue
AARG35
AGLY36
AASN37
AGLY38
AASN97
AALA98

site_idAC9
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 409
ChainResidue
AGLY247
AGLY248
AVAL255
AGLN273
ALEU275
AHOH2274
AHOH2275
AHOH2281
AHOH2295
AHOH2331

site_idBC1
Number of Residues10
DetailsBinding site for Di-peptide VAL A1001 and LYS A1002
ChainResidue
AASN111
AASN112
AALA113
APHE130
AGLU143
ALEU202
AARG203
AHIS231
AZN406
AHOH2332

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
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:4808703
ChainResidueDetails
AGLU143

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:4808703
ChainResidueDetails
AHIS231

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING:
ChainResidueDetails
AASP57
AASP185
AGLU187
AGLU190
ATYR193
ATHR194
AILE197
AASP200
AASP59
AGLN61
AASP138
AHIS142
AHIS146
AGLU166
AGLU177
AASN183

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

226707

PDB entries from 2024-10-30

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