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1LNF

A structural analysis of metal substitutions in thermolysin

Functional Information from GO Data
ChainGOidnamespacecontents
E0004222molecular_functionmetalloendopeptidase activity
E0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE VAL E 1321
ChainResidue
EHIS231
EHOH390
EHOH906
ELYS1322
EASN112
EALA113
EGLU143
EARG203

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE LYS E 1322
ChainResidue
EASN111
EASN112
EVAL1321

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN E 800
ChainResidue
EHIS142
EGLU143
EHIS146
EGLU166
EHOH906
EHOH907

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA E 901
ChainResidue
EASP138
EGLU177
EASP185
EGLU187
EGLU190
EHOH925

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA E 902
ChainResidue
EGLU177
EASN183
EASP185
EGLU190
EHOH905
EHOH908

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA E 903
ChainResidue
EASP57
EASP59
EGLN61
EHOH910
EHOH911
EHOH966

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA E 904
ChainResidue
ETYR193
ETHR194
EILE197
EASP200
EHOH909
EHOH932

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE DMS E 320
ChainResidue
EHIS216
ESER218
ETYR251

site_idZN
Number of Residues5
Details
ChainResidue
EHIS142
EHIS146
EGLU166
EHOH906
EHOH907

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VVAHELTHAV
ChainResidueDetails
EVAL139-VAL148

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING:
ChainResidueDetails
EVAL289
ESER291
ETHR293

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1tlp
ChainResidueDetails
EHIS231
EGLU143

site_idMCSA1
Number of Residues
DetailsM-CSA 176
ChainResidueDetails

226707

PDB entries from 2024-10-30

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