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4K2I

Crystal structure of ntda from bacillus subtilis with bound cofactor pmp

Functional Information from GO Data
ChainGOidnamespacecontents
A0000271biological_processpolysaccharide biosynthetic process
A0003824molecular_functioncatalytic activity
A0008483molecular_functiontransaminase activity
A0017000biological_processantibiotic biosynthetic process
A0030170molecular_functionpyridoxal phosphate binding
B0000271biological_processpolysaccharide biosynthetic process
B0003824molecular_functioncatalytic activity
B0008483molecular_functiontransaminase activity
B0017000biological_processantibiotic biosynthetic process
B0030170molecular_functionpyridoxal phosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues21
DetailsBINDING SITE FOR RESIDUE PMP A 501
ChainResidue
ASER124
ASER242
AASN244
ALYS247
AALA255
ATYR379
AACT509
AHOH620
AHOH622
AHOH686
AHOH770
AGLY125
AHOH856
BASN292
ATHR126
ASER150
APHE151
AALA153
AASP222
ACYS224
AGLN225

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 502
ChainResidue
ATYR246
AARG317
AHIS349
ALEU415
AACT508

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 503
ChainResidue
AASP376
AVAL377
ATYR378
BLYS282
BASN283

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 504
ChainResidue
AVAL119
AHOH786

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 505
ChainResidue
AASN149
APHE175
ATYR199
ALEU382
AHIS407
AVAL410
AHOH607

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 506
ChainResidue
AGLN173
APHE175
ALEU339
APRO340
APRO352
ALYS354
AHOH681

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 507
ChainResidue
AILE381
ALEU382
AMET385
AHIS407

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 508
ChainResidue
ATYR246
ALYS247
AHIS349
ATYR378
AACT502

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT A 509
ChainResidue
ATYR246
APMP501
AHOH622
AHOH856
AHOH875
BTYR274

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 510
ChainResidue
AGLY95
ALYS96
APHE97
ATHR98
ASER99
BPRO245
BTYR246

site_idBC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE PMP B 501
ChainResidue
AASN292
AHOH647
BSER124
BGLY125
BTHR126
BSER150
BALA153
BASP222
BCYS224
BGLN225
BSER242
BASN244
BLYS247
BALA255
BTYR379
BHOH632
BHOH710
BHOH744
BHOH805

site_idBC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 502
ChainResidue
BGLN173
BPHE175
BGLU338
BPRO340
BPRO352
BHOH704
BHOH875

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT B 503
ChainResidue
BTYR246
BARG317
BHIS349
BLEU415

site_idBC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 504
ChainResidue
BASN149
BPHE175
BTYR199
BLEU382
BHIS407
BVAL410
BHOH605

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 505
ChainResidue
ALYS282
AASN283
BASP376
BVAL377
BTYR378

site_idBC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 506
ChainResidue
BTYR118
BVAL119
BHOH837

site_idBC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 507
ChainResidue
BLEU382
BMET385
BHIS407

site_idBC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 508
ChainResidue
APRO245
ATYR246
BGLY95
BLYS96
BPHE97
BTHR98
BSER99

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING:
ChainResidueDetails
ATHR98
AGLY125
AASN244
BTHR98
BGLY125
BASN244

site_idSWS_FT_FI2
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:24097983
ChainResidueDetails
APHE151
BSER242
BTYR274
BLYS282
BASN292
BTYR379
AGLN225
ASER242
ATYR274
ALYS282
AASN292
ATYR379
BPHE151
BGLN225

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine
ChainResidueDetails
ALYS247
BLYS247

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PDB entries from 2024-08-28

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