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4RE0

Crystal structure of VmoLac in P622 space group

Functional Information from GO Data
ChainGOidnamespacecontents
A0008270molecular_functionzinc ion binding
A0009056biological_processcatabolic process
A0016787molecular_functionhydrolase activity
A0016788molecular_functionhydrolase activity, acting on ester bonds
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CO A 401
ChainResidue
AHIS23
AHIS25
AASP257
ACO402
AMYR407
AHOH788

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A 402
ChainResidue
AMYR407
AHOH788
AHIS171
AHIS200
ACO401

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 403
ChainResidue
APHE173
AASP203
ATYR230

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 404
ChainResidue
APHE105
ALYS108
AASN109
ATYR265
AHOH762

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GOL A 405
ChainResidue
ATRP248

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 406
ChainResidue
ALYS177
AASP234
AARG289

site_idAC7
Number of Residues11
DetailsBINDING SITE FOR RESIDUE MYR A 407
ChainResidue
AHIS25
ATYR98
AHIS171
AARG224
AASP257
ATYR265
ATHR273
ACO401
ACO402
AHOH772
AHOH788

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 408
ChainResidue
ASER208
AGLU211
AARG215

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 409
ChainResidue
AHIS161
AILE162
AGLY190
AVAL191
AASP192
AHOH642
AHOH652

Functional Information from PROSITE/UniProt
site_idPS01322
Number of Residues9
DetailsPHOSPHOTRIESTERASE_1 Phosphotriesterase family signature 1. GlTLfHEHL
ChainResidueDetails
AGLY18-LEU26

225946

PDB entries from 2024-10-09

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