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4N3P

Crystal Structure of De Novo designed Serine Hydrolase OSH18, Northeast Structural Genomics Consortium (NESG) Target OR396

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0003866molecular_function3-phosphoshikimate 1-carboxyvinyltransferase activity
A0009073biological_processaromatic amino acid family biosynthetic process
A0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
B0003824molecular_functioncatalytic activity
B0003866molecular_function3-phosphoshikimate 1-carboxyvinyltransferase activity
B0009073biological_processaromatic amino acid family biosynthetic process
B0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA A 501
ChainResidue
AMSE77
AALA78
AGLN180

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 502
ChainResidue
AGLY31
AALA34
AGLY36
ATHR38
AGLY225

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 503
ChainResidue
AGLY258
AGLU260
ALEU263
ANA504
AHOH601
AILE234

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA A 504
ChainResidue
AGLY232
AGLY258
ANA503

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 505
ChainResidue
AVAL40
ATYR41
AASP42
AILE43
AGLY68

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NA A 506
ChainResidue
AHIS10
AILE426

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 507
ChainResidue
ATHR264
AILE267
AASP268
BGLU281
BILE282

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 508
ChainResidue
AASP268
AARG271
BTHR280
BGLU281

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA A 509
ChainResidue
AGLY114
AASP115
ASER119

site_idBC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE NA A 510
ChainResidue
AGLN73

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA A 511
ChainResidue
AGLN346
BLEU128
BTYR161

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 501
ChainResidue
AGLU278
AILE279
BARG271
BILE279

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA B 502
ChainResidue
BVAL229
BASN256
BSER288
BHOH622

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA B 503
ChainResidue
BALA178
BALA181
BGLY183
BSER185
BVAL217

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA B 504
ChainResidue
BVAL40
BTYR41
BASP42
BILE43
BGLY68

site_idBC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NA B 505
ChainResidue
BARG121
BPRO122

site_idBC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA B 506
ChainResidue
BGLU62
BGLN73
BVAL75

site_idBC9
Number of Residues1
DetailsBINDING SITE FOR RESIDUE NA B 507
ChainResidue
BASP233

site_idCC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA B 508
ChainResidue
BGLU314
BPRO316
BILE317
BARG386

site_idCC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PEG B 509
ChainResidue
BILE23
BASP199
BMSE200
BGLN203
BVAL228
BVAL229
BPRO231
BALA286
BHOH614

Functional Information from PROSITE/UniProt
site_idPS00885
Number of Residues19
DetailsEPSP_SYNTHASE_2 EPSP synthase signature 2. KvKETDRIqVVadaLnsMG
ChainResidueDetails
ALYS338-GLY356

250359

PDB entries from 2026-03-11

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