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7KNO

Crystal structure of Acetyl-CoA synthetase in complex with adenosine-5'-ethylphosphate from Cryptococcus neoformans var. grubii serotype A (H99)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003987molecular_functionacetate-CoA ligase activity
A0005524molecular_functionATP binding
A0016208molecular_functionAMP binding
A0016874molecular_functionligase activity
A0019427biological_processacetyl-CoA biosynthetic process from acetate
A0046872molecular_functionmetal ion binding
B0003987molecular_functionacetate-CoA ligase activity
B0005524molecular_functionATP binding
B0016208molecular_functionAMP binding
B0016874molecular_functionligase activity
B0019427biological_processacetyl-CoA biosynthetic process from acetate
B0046872molecular_functionmetal ion binding
C0003987molecular_functionacetate-CoA ligase activity
C0005524molecular_functionATP binding
C0016208molecular_functionAMP binding
C0016874molecular_functionligase activity
C0019427biological_processacetyl-CoA biosynthetic process from acetate
C0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues20
Detailsbinding site for residue WTA A 701
ChainResidue
ATRP334
AMET440
ATHR441
AASP527
AARG542
AHOH827
AHOH1013
AHOH1092
AHOH1195
AHOH1206
AHOH1240
AILE335
AHOH1249
AGLY412
AGLU413
APRO414
AASP436
ATHR437
ATYR438
ATRP439

site_idAC2
Number of Residues6
Detailsbinding site for residue EDO A 702
ChainResidue
AALA320
AHIS321
APRO322
AASN348
AHOH1071
AHOH1076

site_idAC3
Number of Residues5
Detailsbinding site for residue PO4 A 703
ChainResidue
ALYS297
AARG510
ATHR514
AHOH1230
AHOH1261

site_idAC4
Number of Residues5
Detailsbinding site for residue PO4 A 704
ChainResidue
AHIS43
ALYS315
ATYR316
AHOH830
AHOH1147

site_idAC5
Number of Residues7
Detailsbinding site for residue EDO A 705
ChainResidue
ALYS82
AHOH862
AHOH1182
CASP76
CTRP77
CTYR78
CTYR106

site_idAC6
Number of Residues5
Detailsbinding site for residue EDO B 701
ChainResidue
AASP76
ATRP77
BLYS82
BHOH827
BHOH1204

site_idAC7
Number of Residues21
Detailsbinding site for residue WTA B 702
ChainResidue
BTRP334
BILE335
BVAL411
BGLY412
BGLU413
BPRO414
BASP436
BTHR437
BTYR438
BTRP439
BMET440
BTHR441
BASP527
BILE539
BARG542
BHOH868
BHOH1098
BHOH1123
BHOH1233
BHOH1269
BHOH1282

site_idAC8
Number of Residues5
Detailsbinding site for residue EDO B 703
ChainResidue
BASP76
BTRP77
BHOH921
BHOH1028
CGLU99

site_idAC9
Number of Residues7
Detailsbinding site for residue EDO B 704
ChainResidue
BLYS315
BALA320
BHIS321
BPRO322
BASN348
BHOH822
BHOH1266

site_idAD1
Number of Residues4
Detailsbinding site for residue EDO B 705
ChainResidue
BTYR48
BASP534
BHOH1114
BHOH1273

site_idAD2
Number of Residues4
Detailsbinding site for residue PO4 B 706
ChainResidue
BLYS297
BARG510
BTHR514
BHOH1262

site_idAD3
Number of Residues4
Detailsbinding site for residue PO4 B 707
ChainResidue
BHIS43
BLYS315
BTYR316
BHOH881

site_idAD4
Number of Residues15
Detailsbinding site for residue WTA C 701
ChainResidue
CTYR438
CTRP439
CMET440
CTHR441
CASP527
CILE539
CARG542
CARG553
CHOH1000
CVAL411
CGLY412
CGLU413
CPRO414
CASP436
CTHR437

site_idAD5
Number of Residues5
Detailsbinding site for residue EDO C 702
ChainResidue
CLYS315
CALA320
CHIS321
CPRO322
CASN348

site_idAD6
Number of Residues1
Detailsbinding site for residue EDO C 703
ChainResidue
CARG218

site_idAD7
Number of Residues3
Detailsbinding site for residue PO4 C 704
ChainResidue
CHIS43
CLYS315
CTYR316

Functional Information from PROSITE/UniProt
site_idPS00455
Number of Residues12
DetailsAMP_BINDING Putative AMP-binding domain signature. ILYTSGSTGkPK
ChainResidueDetails
AILE286-LYS297

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PDB entries from 2024-07-10

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