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5O8N

Structure of thermolysin at room temperature via a method of acoustically induced rotation.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue CA A 401
ChainResidue
AASP138
AGLU177
AASP185
AGLU187
AGLU190
AHOH524

site_idAC2
Number of Residues6
Detailsbinding site for residue CA A 402
ChainResidue
AHOH504
AHOH550
AHOH564
AASP57
AASP59
AGLN61

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN A 403
ChainResidue
AHIS142
AHIS146
AGLU166
ACL404

site_idAC4
Number of Residues8
Detailsbinding site for residue CL A 404
ChainResidue
AHIS142
AHIS146
ATYR157
AGLU166
AHIS231
AZN403
ACL406
AHOH602

site_idAC5
Number of Residues1
Detailsbinding site for residue CL A 405
ChainResidue
AHOH606

site_idAC6
Number of Residues2
Detailsbinding site for residue CL A 406
ChainResidue
ACL404
AHOH602

site_idAC7
Number of Residues1
Detailsbinding site for residue NA A 407
ChainResidue
AGLN246

site_idAC8
Number of Residues1
Detailsbinding site for residue NA A 408
ChainResidue
AASN19

site_idAC9
Number of Residues2
Detailsbinding site for residue NA A 409
ChainResidue
AARG35
AHOH586

site_idAD1
Number of Residues6
Detailsbinding site for residue NA A 411
ChainResidue
ASER298
ASER298
AHOH557
AHOH557
AHOH605
AHOH605

site_idAD2
Number of Residues6
Detailsbinding site for residue CA A 412
ChainResidue
ATYR193
ATHR194
AILE197
AASP200
AHOH502
AHOH549

site_idAD3
Number of Residues5
Detailsbinding site for residue CA A 413
ChainResidue
AGLU177
AASN183
AASP185
AGLU190
AASP191

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
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:4808703
ChainResidueDetails
AGLU143

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:4808703
ChainResidueDetails
AHIS231

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING:
ChainResidueDetails
AGLN61
AASP138
AHIS142
AHIS146
AGLU166
AGLU177
AASN183
AASP185
AGLU187
AGLU190
ATYR193
ATHR194
AILE197
AASP200
AASP57
AASP59

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

218500

PDB entries from 2024-04-17

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