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6FJ2

Structure of Thermolysin solved from SAD data collected at the peak of the Zn absorption edge on ID30B

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 1401
ChainResidue
AHIS142
AHIS146
AGLU166
AHOH1749

site_idAC2
Number of Residues6
Detailsbinding site for residue CA A 1402
ChainResidue
AHOH1739
ATYR193
ATHR194
AILE197
AASP200
AHOH1601

site_idAC3
Number of Residues7
Detailsbinding site for residue CA A 1403
ChainResidue
AASP138
AGLU177
AASP185
AGLU187
AGLU190
ACA1405
AHOH1616

site_idAC4
Number of Residues6
Detailsbinding site for residue CA A 1404
ChainResidue
AASP57
AASP59
AGLN61
AHOH1613
AHOH1621
AHOH1768

site_idAC5
Number of Residues6
Detailsbinding site for residue CA A 1405
ChainResidue
AGLU177
AASN183
AASP185
AGLU190
ACA1403
AHOH1529

site_idAC6
Number of Residues2
Detailsbinding site for residue DMS A 1406
ChainResidue
ATYR66
ASER218

site_idAC7
Number of Residues6
Detailsbinding site for residue TMO A 1407
ChainResidue
ALEU50
ATYR93
AGLY117
ASER118
ATYR151
AHOH1546

site_idAC8
Number of Residues5
Detailsbinding site for residue TMO A 1408
ChainResidue
APHE63
APHE63
ASER65
AHOH1517
AHOH1517

site_idAC9
Number of Residues4
Detailsbinding site for residue TMO A 1409
ChainResidue
AARG285
ALYS307
AHOH1670
AHOH1814

site_idAD1
Number of Residues3
Detailsbinding site for residue TMO A 1410
ChainResidue
AASP94
AGLY95
ATYR242

site_idAD2
Number of Residues7
Detailsbinding site for residue VAL A 1411
ChainResidue
AASN112
AALA113
AGLU143
AARG203
AHIS231
ALYS1412
AHOH1545

site_idAD3
Number of Residues8
Detailsbinding site for residue LYS A 1412
ChainResidue
AASN111
AASN112
ALEU202
AHIS231
AVAL1411
AHOH1545
AHOH1612
AHOH1646

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
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"4808703","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"4808703","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {}
ChainResidueDetails

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

238895

PDB entries from 2025-07-16

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