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2DH5

Crystal structure of E. coli Holo-TrpB

Functional Information from GO Data
ChainGOidnamespacecontents
A0000162biological_processtryptophan biosynthetic process
A0004834molecular_functiontryptophan synthase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006568biological_processtryptophan metabolic process
A0009073biological_processaromatic amino acid family biosynthetic process
A0016829molecular_functionlyase activity
A0030170molecular_functionpyridoxal phosphate binding
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 801
ChainResidue
APRO23
AARG26
AGLN27

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 802
ChainResidue
AHIS115
ALYS87
ATHR110
AGLY111
AALA112
AGLY113
AGLN114

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE PLP A 501
ChainResidue
AHIS86
ALYS87
ATHR190
ACYS230
AGLY232
AGLY233
AGLY234
ASER235
AASN236
AGLY303
AALA348
AGLU350
ASER377
AGLY378

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 901
ChainResidue
AHIS82
AGLY83
AVAL117
AILE345
AILE346
AARG379
AASP381

Functional Information from PROSITE/UniProt
site_idPS00168
Number of Residues15
DetailsTRP_SYNTHASE_BETA Tryptophan synthase beta chain pyridoxal-phosphate attachment site. LlHgGAHKtNqvLgQ
ChainResidueDetails
ALEU80-GLN94

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:6985892
ChainResidueDetails
ACYS62

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:6985892
ChainResidueDetails
AHIS86

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250
ChainResidueDetails
ALYS87

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a50
ChainResidueDetails
AHIS86
ALYS87
ALYS167
AASP305

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a50
ChainResidueDetails
ALYS87

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a50
ChainResidueDetails
ASER377
ALYS87

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PDB entries from 2024-07-24

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