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4XEO

Crystal Structure of human AlaRS catalytic domain with R329H mutation

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003676molecular_functionnucleic acid binding
A0004813molecular_functionalanine-tRNA ligase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006419biological_processalanyl-tRNA aminoacylation
B0000166molecular_functionnucleotide binding
B0003676molecular_functionnucleic acid binding
B0004813molecular_functionalanine-tRNA ligase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006419biological_processalanyl-tRNA aminoacylation
Functional Information from PDB Data
site_idAC1
Number of Residues19
Detailsbinding site for residue A5A A 501
ChainResidue
AALA44
AILE214
AASN216
AVAL218
AASP239
ATHR240
AGLY241
AGLY243
AARG246
AHOH689
AHOH695
AARG77
ATYR93
AHIS94
AHIS95
APHE98
AMET100
ATRP176
AGLU213

site_idAC2
Number of Residues11
Detailsbinding site for residue GOL A 502
ChainResidue
AHIS27
ASER28
ASER29
AALA30
ALYS74
AGLU363
AHOH721
AHOH736
AHOH831
AHOH867
BGLU268

site_idAC3
Number of Residues4
Detailsbinding site for residue GOL A 503
ChainResidue
AGLN12
AILE15
ALYS19
AHOH826

site_idAC4
Number of Residues6
Detailsbinding site for residue SO4 A 504
ChainResidue
ATYR109
APHE110
AGLU112
ALEU113
AHOH763
AHOH845

site_idAC5
Number of Residues4
Detailsbinding site for residue SO4 A 505
ChainResidue
AASP86
AARG330
AARG333
ATYR334

site_idAC6
Number of Residues6
Detailsbinding site for residue MG A 506
ChainResidue
AGLU189
AGLU213
AHOH784
AHOH820
AHOH863
AHOH1016

site_idAC7
Number of Residues21
Detailsbinding site for residue A5A B 501
ChainResidue
BALA44
BARG77
BTYR93
BHIS94
BHIS95
BPHE98
BMET100
BTRP176
BGLU213
BILE214
BASN216
BVAL218
BASP239
BTHR240
BGLY241
BGLY243
BARG246
BHOH651
BHOH653
BHOH747
BHOH893

site_idAC8
Number of Residues4
Detailsbinding site for residue GOL B 502
ChainResidue
BGLN12
BILE15
BLYS19
BHOH605

site_idAC9
Number of Residues11
Detailsbinding site for residue GOL B 503
ChainResidue
AGLU268
BHIS27
BSER28
BSER29
BALA30
BLYS74
BGLU363
BHOH601
BHOH608
BHOH610
BHOH614

site_idAD1
Number of Residues4
Detailsbinding site for residue SO4 B 504
ChainResidue
BASP86
BARG330
BARG333
BTYR334

site_idAD2
Number of Residues6
Detailsbinding site for residue SO4 B 505
ChainResidue
BTYR109
BPHE110
BGLU112
BLEU113
BHOH713
BHOH968

site_idAD3
Number of Residues6
Detailsbinding site for residue MG B 506
ChainResidue
BHOH771
BHOH976
BHOH977
BGLU189
BGLU213
BHOH714

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:27622773, ECO:0000269|Ref.24, ECO:0007744|PDB:4XEM, ECO:0007744|PDB:4XEO, ECO:0007744|PDB:5KNN
ChainResidueDetails
AARG77
BTRP176
BILE214
BASN216
BASP239
BGLY243
AHIS95
ATRP176
AILE214
AASN216
AASP239
AGLY243
BARG77
BHIS95

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N-acetylmethionine => ECO:0000255|HAMAP-Rule:MF_03133, ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378
ChainResidueDetails
AMET1
BMET1

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER3
ASER8
BSER3
BSER8

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS19
BLYS19

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231
ChainResidueDetails
ASER399
BSER399

222415

PDB entries from 2024-07-10

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