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4N4E

Thermolysin in complex with UBTLN58

Functional Information from GO Data
ChainGOidnamespacecontents
E0004222molecular_functionmetalloendopeptidase activity
E0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN E 401
ChainResidue
EHIS142
EHIS146
EGLU166
E2G6412

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA E 402
ChainResidue
EHOH501
EASP138
EGLU177
EASP185
EGLU187
EGLU190

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA E 403
ChainResidue
EASP57
EASP59
EGLN61
EHOH519
EHOH527
EHOH552

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA E 404
ChainResidue
ETYR193
ETHR194
EILE197
EASP200
EHOH556
EHOH608

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA E 405
ChainResidue
EGLU177
EASN183
EASP185
EGLU190
EHOH573
EHOH587

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE DMS E 406
ChainResidue
EILE1
ETHR2
EGLY3
EGLN31
EASN33

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE DMS E 407
ChainResidue
ETYR66
EHIS216
ESER218
ETYR251
EHOH566

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE DMS E 408
ChainResidue
ETYR110
EASN112
EPHE114
E2G6412
E2G6412

site_idAC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL E 409
ChainResidue
EGLY109
ETYR110
EASN111
EASN112
EGLN158
EASN227
EHOH591
EHOH643
EHOH671

site_idBC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL E 410
ChainResidue
EPHE114
ETRP115
EHIS146
ETYR157
E2G6412
EHOH518
EHOH553
EHOH844

site_idBC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GOL E 411
ChainResidue
EGLY247
EGLY248
ETHR249
EVAL255
EGLN273
ETYR274
ELEU275
ETHR276
EHOH555
EHOH602
EHOH620
EHOH624

site_idBC3
Number of Residues19
DetailsBINDING SITE FOR RESIDUE 2G6 E 412
ChainResidue
ETYR106
EASN112
EALA113
EPHE114
ETRP115
EHIS142
EGLU143
EHIS146
ETYR157
EGLU166
ELEU202
EARG203
EHIS231
EZN401
EDMS408
EDMS408
EGOL410
EHOH535
EHOH769

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

237735

PDB entries from 2025-06-18

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