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5FSJ

Structure of thermolysin prepared by the 'soak-and-freeze' method under 45 bar of oxygen 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 1003
ChainResidue
ATYR193
ATHR194
AILE197
AASP200
AHOH2371
AHOH2375

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1004
ChainResidue
AGLU190
AHOH2353
AHOH2361
AGLU177
AASN183
AASP185

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1005
ChainResidue
AASP59
AGLN61
ACA1010
AHOH2172
AHOH2179
AHOH2545

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ZN A 1006
ChainResidue
AHIS142
AHIS146
ATYR157
AGLU166
AHIS231
AVAL1001
AZN1007

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1007
ChainResidue
AHIS142
AHIS146
AGLU166
AZN1006

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE OXY A 1008
ChainResidue
ATYR84
ASER92
ATYR93
AILE100
ALEU144

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1009
ChainResidue
AASP138
AGLU177
AASP185
AGLU187
AGLU190
AHOH2318

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1010
ChainResidue
AASP57
AASP59
AGLN61
ACA1005
AHOH2171
AHOH2172

site_idAC9
Number of Residues13
DetailsBinding site for Di-peptide VAL A1001 and LYS A1002
ChainResidue
AASN111
AASN112
AALA113
APHE130
AGLU143
ALEU202
AARG203
AHIS231
AZN1006
AHOH2435
AHOH2541
AHOH2542
AHOH2544

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

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PDB entries from 2024-10-30

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