Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3DO1

Thermolysin by Classical hanging drop method before high X-Ray dose on ESRF ID14-2 beamline

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
AHOH1005

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 402
ChainResidue
AGLU190
AHOH1019
AHOH1030
AGLU177
AASN183
AASP185

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 403
ChainResidue
AASP57
AASP59
AGLN61
AHOH1014
AHOH1016
AHOH1021

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 404
ChainResidue
ATYR193
ATHR194
AILE197
AASP200
AHOH1009
AHOH1051

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 405
ChainResidue
AHIS142
AHIS146
AGLU166

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE VAL A 1001
ChainResidue
AASN112
AALA113
AGLU143
AARG203
AHIS231
ALYS1002
AHOH1185

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE LYS A 1002
ChainResidue
AASN111
AASN112
APHE130
AHIS231
AHOH1164

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
AASP57
AASP185
AGLU187
AGLU190
ATYR193
ATHR194
AILE197
AASP200
AASP59
AGLN61
AASP138
AHIS142
AHIS146
AGLU166
AGLU177
AASN183

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1tlp
ChainResidueDetails
AHIS231
AGLU143

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

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon