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3ELE

Crystal structure of Amino Transferase (RER070207001803) from Eubacterium rectale at 2.10 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0008483molecular_functiontransaminase activity
A0009058biological_processbiosynthetic process
A0030170molecular_functionpyridoxal phosphate binding
B0003824molecular_functioncatalytic activity
B0008483molecular_functiontransaminase activity
B0009058biological_processbiosynthetic process
B0030170molecular_functionpyridoxal phosphate binding
C0003824molecular_functioncatalytic activity
C0008483molecular_functiontransaminase activity
C0009058biological_processbiosynthetic process
C0030170molecular_functionpyridoxal phosphate binding
D0003824molecular_functioncatalytic activity
D0008483molecular_functiontransaminase activity
D0009058biological_processbiosynthetic process
D0030170molecular_functionpyridoxal phosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PLP A 500
ChainResidue
AGLY106
ASER246
ALYS247
AARG255
BTYR71
AALA107
AALA108
APHE133
AASN178
AASN182
AASP216
ATYR219
ASER244

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE PLP B 500
ChainResidue
ATYR71
BGLY106
BALA107
BALA108
BPHE133
BASN178
BASN182
BASP216
BTYR219
BSER244
BSER246
BLYS247
BARG255
BHOH611

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PLP C 500
ChainResidue
CGLY106
CALA107
CALA108
CPHE133
CASN178
CASN182
CASP216
CTYR219
CSER244
CSER246
CLYS247
CARG255
DTYR71

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PLP D 500
ChainResidue
CTYR71
DGLY106
DALA107
DALA108
DASN178
DASN182
DASP216
DTYR219
DSER244
DSER246
DLYS247
DARG255

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 501
ChainResidue
BASN141
BARG146
BLEU147
BEDO510

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL D 501
ChainResidue
DLYS137
DASN141
DARG146
DLEU147

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 501
ChainResidue
ATYR243
AGLN299
AGLY300
AALA301
ATHR302
AHOH705
AHOH969

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO B 502
ChainResidue
AHOH737
AHOH868
BGLU221
BTYR243
BGLN299
BGLY300
BALA301
BTHR302

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO C 501
ChainResidue
CPHE87
CTYR243
CSER248
CGLY300
CALA301
CTHR302
CHOH776

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 503
ChainResidue
AHOH598
AHOH771
BSER204
BARG209
BPRO210
BHOH617

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 502
ChainResidue
ATYR23
AARG27
AGLU353

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 504
ChainResidue
BGLU125
BARG146
BHOH578
BHOH597
BHOH602
CARG146

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 505
ChainResidue
BVAL376
BASP377
BARG378
BSER45
BASN311

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 506
ChainResidue
BGLY42
BPHE133
BASN182
BTYR334
BARG371

site_idBC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO B 507
ChainResidue
AHOH561
BALA170

site_idBC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 508
ChainResidue
ATYR8
BASP267
BGLU270
BPRO386
BGLU389
BLYS393

site_idBC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 509
ChainResidue
BLYS137
BLEU147
BGLU149

site_idBC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 510
ChainResidue
BLYS137
BASN141
BARG146
BCL501
CTYR123
CHIS171

Functional Information from PROSITE/UniProt
site_idPS00105
Number of Residues14
DetailsAA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SYSKslSLpGERIG
ChainResidueDetails
ASER244-GLY257

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PDB entries from 2024-05-15

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