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3MSA

Crystal structure of Thermolysin in complex with 3-Bromophenol

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 B3R A 401
ChainResidue
AASN112
AALA113
APHE130
ALEU133
AHIS142
AGLU143
ALEU202
AHOH1047

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE B3R A 402
ChainResidue
ASER92
ATYR93
AILE100
ALEU144
AVAL148
ATYR84

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 501
ChainResidue
AHIS142
AGLU143
AHIS146
AGLU166
AHOH1171

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 601
ChainResidue
AASP138
AGLU177
AASP185
AGLU187
AGLU190
AHOH1019

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 602
ChainResidue
AGLU177
AASN183
AASP185
AGLU190
AHOH1072
AHOH1143

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 603
ChainResidue
AASP57
AASP59
AGLN61
AHOH1059
AHOH1065
AHOH1174

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 604
ChainResidue
ATYR193
ATHR194
AILE197
AASP200
AHOH1158
AHOH1186

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 701
ChainResidue
AVAL13
AILE131
APRO132
AHOH1216

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 702
ChainResidue
APHE114
APHE114
ATRP115
AASN116
AASN116

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE IPA A 801
ChainResidue
APHE114
ATRP115
AGLU143
AHOH1079

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 2024-07-17

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