Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6SC0

THERMOLYSIN IN COMPLEX WITH FRAGMENT J22

Functional Information from GO Data
ChainGOidnamespacecontents
E0004222molecular_functionmetalloendopeptidase activity
E0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue CA E 401
ChainResidue
EASP138
EGLU177
EASP185
EGLU187
EGLU190
EHOH557

site_idAC2
Number of Residues6
Detailsbinding site for residue CA E 402
ChainResidue
EGLU190
EHOH547
EHOH573
EGLU177
EASN183
EASP185

site_idAC3
Number of Residues6
Detailsbinding site for residue CA E 403
ChainResidue
EASP57
EASP59
EGLN61
EHOH556
EHOH581
EHOH713

site_idAC4
Number of Residues6
Detailsbinding site for residue CA E 404
ChainResidue
ETYR193
ETHR194
EILE197
EASP200
EHOH564
EHOH688

site_idAC5
Number of Residues4
Detailsbinding site for residue ZN E 405
ChainResidue
EHIS142
EHIS146
EGLU166
EBCT410

site_idAC6
Number of Residues5
Detailsbinding site for residue TRS E 406
ChainResidue
ELEU202
EARG203
EASP213
EHIS231
EHOH501

site_idAC7
Number of Residues5
Detailsbinding site for residue DMS E 407
ChainResidue
EGLY95
EPRO184
EASP185
ETRP186
EHOH505

site_idAC8
Number of Residues2
Detailsbinding site for residue IPA E 408
ChainResidue
EASN37
EALA99

site_idAC9
Number of Residues9
Detailsbinding site for residue L5Q E 409
ChainResidue
EASN112
EALA113
ELEU133
EVAL139
EGLU143
ELEU202
EARG203
EHIS231
EBCT410

site_idAD1
Number of Residues10
Detailsbinding site for residue BCT E 410
ChainResidue
EALA113
EHIS142
EGLU143
EHIS146
ETYR157
EGLU166
EHIS231
EZN405
EL5Q409
EHOH671

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
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:4808703
ChainResidueDetails
EGLU143

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:4808703
ChainResidueDetails
EHIS231

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING:
ChainResidueDetails
EASP57
EASP185
EGLU187
EGLU190
ETYR193
ETHR194
EILE197
EASP200
EASP59
EGLN61
EASP138
EHIS142
EHIS146
EGLU166
EGLU177
EASN183

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 176
ChainResidueDetails

238268

PDB entries from 2025-07-02

PDB statisticsPDBj update infoContact PDBjnumon