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3KGX

Crystal structure of Putative aminotransferase (AAH25799.1) from MUS MUSCULUS at 1.80 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004760molecular_functionserine-pyruvate transaminase activity
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0005777cellular_componentperoxisome
A0005782cellular_componentperoxisomal matrix
A0006563biological_processL-serine metabolic process
A0007219biological_processNotch signaling pathway
A0008453molecular_functionalanine-glyoxylate transaminase activity
A0008483molecular_functiontransaminase activity
A0009436biological_processglyoxylate catabolic process
A0016597molecular_functionamino acid binding
A0019265biological_processglycine biosynthetic process, by transamination of glyoxylate
A0019448biological_processL-cysteine catabolic process
A0030170molecular_functionpyridoxal phosphate binding
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0042853biological_processL-alanine catabolic process
A0042866biological_processpyruvate biosynthetic process
A0043231cellular_componentintracellular membrane-bounded organelle
A0043621molecular_functionobsolete protein self-association
A0046487biological_processglyoxylate metabolic process
A0046724biological_processoxalic acid secretion
A0051384biological_processresponse to glucocorticoid
A0051591biological_processresponse to cAMP
B0004760molecular_functionserine-pyruvate transaminase activity
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0005777cellular_componentperoxisome
B0005782cellular_componentperoxisomal matrix
B0006563biological_processL-serine metabolic process
B0007219biological_processNotch signaling pathway
B0008453molecular_functionalanine-glyoxylate transaminase activity
B0008483molecular_functiontransaminase activity
B0009436biological_processglyoxylate catabolic process
B0016597molecular_functionamino acid binding
B0019265biological_processglycine biosynthetic process, by transamination of glyoxylate
B0019448biological_processL-cysteine catabolic process
B0030170molecular_functionpyridoxal phosphate binding
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0042853biological_processL-alanine catabolic process
B0042866biological_processpyruvate biosynthetic process
B0043231cellular_componentintracellular membrane-bounded organelle
B0043621molecular_functionobsolete protein self-association
B0046487biological_processglyoxylate metabolic process
B0046724biological_processoxalic acid secretion
B0051384biological_processresponse to glucocorticoid
B0051591biological_processresponse to cAMP
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 502
ChainResidue
AASN54
ALEU55
AHOH789
BMET67

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 503
ChainResidue
AHIS319
AHIS323
AASP396
AHOH678
AHOH679

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 504
ChainResidue
AGLU315
ATHR392
AHOH700
AHOH744
BARG403
BHOH740

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 505
ChainResidue
APHE113
ALEU116
AGLU117
APRO118
AILE141
AARG255
APRO259
AVAL260

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 507
ChainResidue
AARG93
APRO95
AVAL145
AASP246
AHOH603
AHOH626
AHOH813

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 508
ChainResidue
APRO187
ALEU188
AASP189
AHOH628
AHOH801
AHOH820

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 510
ChainResidue
AGLU109
BGLU109
BHOH665

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 511
ChainResidue
AGLY190
AHOH672
AHOH681
BARG255

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL B 501
ChainResidue
AARG66
AMET67
BASN54
BLEU55
BHOH768

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 506
ChainResidue
BPHE113
BLEU116
BGLU117
BILE141
BARG255
BPRO259
BVAL260

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 509
ChainResidue
BILE129
BARG133
BHOH671

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 512
ChainResidue
BLEU188
BASP189
BHOH620
BHOH758
BHOH814

Functional Information from PROSITE/UniProt
site_idPS00595
Number of Residues21
DetailsAA_TRANSFER_CLASS_5 Aminotransferases class-V pyridoxal-phosphate attachment site. IDIMysSSQKvlnappGiSlI
ChainResidueDetails
AILE222-ILE242

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AARG382
BARG382

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250
ChainResidueDetails
ALYS231
BLYS231

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0007744|PubMed:23806337
ChainResidueDetails
ALYS247
ALYS330
BLYS247
BLYS330

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:23576753
ChainResidueDetails
ALYS256
ALYS334
BLYS256
BLYS334

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1b8g
ChainResidueDetails
ALYS231
ATRP130
AASP205

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1b8g
ChainResidueDetails
BLYS231
BTRP130
BASP205

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1b8g
ChainResidueDetails
ALYS251
ATRP130
AASP205

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1b8g
ChainResidueDetails
BLYS251
BTRP130
BASP205

site_idCSA5
Number of Residues1
DetailsAnnotated By Reference To The Literature 1b8g
ChainResidueDetails
ALYS73

site_idCSA6
Number of Residues1
DetailsAnnotated By Reference To The Literature 1b8g
ChainResidueDetails
BLYS73

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PDB entries from 2024-07-24

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