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4RDZ

Crystal structure of VmoLac in P64 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
B0008270molecular_functionzinc ion binding
B0009056biological_processcatabolic process
B0016787molecular_functionhydrolase activity
B0016788molecular_functionhydrolase activity, acting on ester bonds
B0046872molecular_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
AMYR404
AHOH985

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CO A 402
ChainResidue
ACO401
AMYR404
AHOH985
AHIS171
AHIS200
AARG224

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 403
ChainResidue
ATHR99
ATYR100
ATRP264
AHOH519
AHOH531
AHOH587
AHOH607
AHOH678
BPHE105

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE MYR A 404
ChainResidue
AHIS25
ATYR98
AHIS171
AARG224
AILE229
AASP257
ATRP264
ACO401
ACO402
AHOH985

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CO B 401
ChainResidue
BHIS23
BHIS25
BASP257
BCO402
BMYR404
BHOH1007

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CO B 402
ChainResidue
BHIS171
BHIS200
BARG224
BCO401
BMYR404
BHOH1007

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 403
ChainResidue
BGLU211
BARG215
BARG246
BHOH722
BHOH808

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MYR B 404
ChainResidue
BHIS25
BTYR98
BHIS171
BARG224
BASP257
BTRP264
BCO401
BCO402
BHOH1007

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

218853

PDB entries from 2024-04-24

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