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4N5P

Thermolysin in complex with UBTLN20

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
EHOH601

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA E 402
ChainResidue
EHOH620
EHOH624
EHOH635
EASP57
EASP59
EGLN61

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA E 403
ChainResidue
EGLU177
EASN183
EASP185
EGLU190
EHOH897
EHOH974

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA E 404
ChainResidue
ETYR193
ETHR194
EILE197
EASP200
EHOH642
EHOH697

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN E 405
ChainResidue
EHIS142
EHIS146
EGLU166
E2H0412

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL E 406
ChainResidue
EPHE114
ETRP115
EHIS146
ETYR157
E2H0412
EHOH607
EHOH656
EHOH943

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE DMS E 407
ChainResidue
EILE1
ETHR2
EGLY3
EGLN31
EASN33

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL E 408
ChainResidue
EGLY109
ETYR110
EASN111
EASN112
EGLN158
EHOH714
EHOH878
EHOH900
EHOH1065

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE DMS E 409
ChainResidue
EGLY95
EPRO184
ETRP186
EHOH676
EHOH829

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE DMS E 410
ChainResidue
ETYR110
EASN112
EPHE114
E2H0412
E2H0412

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE DMS E 411
ChainResidue
ETYR66
EHIS216
ESER218
ETYR251
EHOH668
EHOH988

site_idBC3
Number of Residues21
DetailsBINDING SITE FOR RESIDUE 2H0 E 412
ChainResidue
ETYR106
EASN111
EASN112
EALA113
EPHE114
ETRP115
EPHE130
EHIS142
EGLU143
EHIS146
ETYR157
EGLU166
ELEU202
EARG203
EHIS231
EZN405
EGOL406
EDMS410
EDMS410
EHOH671
EHOH1053

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

246704

PDB entries from 2025-12-24

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