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1KEI

Thermolysin (substrate-free)

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
AHOH1005

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 402
ChainResidue
AGLU190
AHOH1019
AHOH1030
AGLU177
AASN183
AASP185

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 403
ChainResidue
AASP57
AASP59
AGLN61
AHOH1014
AHOH1016
AHOH1021

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 404
ChainResidue
ATYR193
ATHR194
AILE197
AASP200
AHOH1009
AHOH1051

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 405
ChainResidue
AHIS142
AHIS146
AGLU166

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE VAL A 1001
ChainResidue
AASN112
AALA113
AGLU143
AARG203
AHIS231
ALYS1002
AHOH1185

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE LYS A 1002
ChainResidue
AASN112
APHE130
ALEU202
AHIS231
AVAL1001
AHOH1164

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 Residues3
DetailsBINDING:
ChainResidueDetails
AVAL289
ASER291
ATHR293

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1tlp
ChainResidueDetails
AHIS231
AGLU143

site_idMCSA1
Number of Residues
DetailsM-CSA 176
ChainResidueDetails

226707

PDB entries from 2024-10-30

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