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6SC1

THERMOLYSIN IN COMPLEX WITH FRAGMENT J96

Functional Information from GO Data
ChainGOidnamespacecontents
E0004222molecular_functionmetalloendopeptidase activity
E0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue ZN E 401
ChainResidue
EHIS142
EGLU143
EHIS146
EGLU166
EL5W406

site_idAC2
Number of Residues6
Detailsbinding site for residue CA E 402
ChainResidue
EHOH591
EHOH678
EASP57
EASP59
EGLN61
EHOH571

site_idAC3
Number of Residues6
Detailsbinding site for residue CA E 403
ChainResidue
EGLU177
EASN183
EASP185
EGLU190
EHOH540
EHOH552

site_idAC4
Number of Residues6
Detailsbinding site for residue CA E 404
ChainResidue
ETYR193
ETHR194
EILE197
EASP200
EHOH562
EHOH662

site_idAC5
Number of Residues6
Detailsbinding site for residue CA E 405
ChainResidue
EASP138
EGLU177
EASP185
EGLU187
EGLU190
EHOH550

site_idAC6
Number of Residues12
Detailsbinding site for residue L5W E 406
ChainResidue
EASN112
EALA113
EHIS142
EGLU143
EHIS146
ETYR157
EGLU166
ELEU202
EARG203
EHIS231
EZN401
EGOL410

site_idAC7
Number of Residues5
Detailsbinding site for residue IPA E 407
ChainResidue
ETHR4
ETYR28
EASP59
EASN60
EHOH609

site_idAC8
Number of Residues4
Detailsbinding site for residue GOL E 408
ChainResidue
EASN96
EGLU187
EGLY199
EASP200

site_idAC9
Number of Residues5
Detailsbinding site for residue GOL E 409
ChainResidue
ESER25
ETYR29
EGLY212
EASP213
EGOL411

site_idAD1
Number of Residues6
Detailsbinding site for residue GOL E 410
ChainResidue
ETRP115
EGLU143
EHIS146
ETYR157
EL5W406
EHOH525

site_idAD2
Number of Residues6
Detailsbinding site for residue GOL E 411
ChainResidue
ELEU202
EARG203
EASP213
EHIS231
EGOL409
EHOH535

site_idAD3
Number of Residues5
Detailsbinding site for residue DMS E 412
ChainResidue
EGLY95
EPRO184
ETRP186
EHOH542
EHOH650

site_idAD4
Number of Residues4
Detailsbinding site for residue DMS E 413
ChainResidue
ETHR2
EGLY3
EGLN31
EASN33

site_idAD5
Number of Residues4
Detailsbinding site for residue DMS E 414
ChainResidue
EGLY259
EARG260
EASP261
EHOH584

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 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

246031

PDB entries from 2025-12-10

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