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3T8G

Thermolysin In Complex With UBTLN26

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE UBT A 401
ChainResidue
ATYR106
AGLU166
AARG203
AHIS231
AGOL404
ADMS406
ADMS406
AZN411
AHOH852
AHOH858
AHOH875
AASN112
AALA113
APHE114
ATRP115
AHIS142
AGLU143
AHIS146
ATYR157

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 402
ChainResidue
AGLY247
AGLY248
AVAL255
AGLN273
ALEU275
AHOH670
AHOH680
AHOH705
AHOH753
AHOH864

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 403
ChainResidue
ASER65
ATYR66
APRO69
AHIS105
AASP124
AHOH577
AHOH850
AHOH871

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 404
ChainResidue
APHE114
ATRP115
AHIS146
ATYR157
AUBT401
AHOH621
AHOH657
AHOH676

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 405
ChainResidue
AGLY109
ATYR110
AASN111
AASN112
AGLN158
ADMS406
AHOH671
AHOH800
AHOH867

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE DMS A 406
ChainResidue
ATYR110
AASN112
APHE114
AUBT401
AUBT401
AGOL405
AHOH730

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE DMS A 407
ChainResidue
AILE1
ATHR2
AGLY3
AGLN31
AASN33

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE DMS A 408
ChainResidue
ATYR24
ASER25

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DMS A 409
ChainResidue
ATYR66
AHIS216
ATYR251
AHOH767

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE DMS A 410
ChainResidue
AGLY95
APRO184
ATRP186
AHOH686
AHOH848

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 411
ChainResidue
AHIS142
AHIS146
AGLU166
AUBT401

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 412
ChainResidue
AASP138
AGLU177
AASP185
AGLU187
AGLU190
AHOH907

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 413
ChainResidue
AGLU177
AASN183
AASP185
AGLU190
AHOH912
AHOH913

site_idBC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 414
ChainResidue
ATYR193
ATHR194
AILE197
AASP200
AHOH910
AHOH914

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 415
ChainResidue
AASP57
AASP59
AGLN61
AHOH908
AHOH909
AHOH911

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

222926

PDB entries from 2024-07-24

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