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6MFU

Crystal structure of a Guanylate kinase from Cryptococcus neoformans var. grubii serotype A in complex with GDP and ADP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004385molecular_functionGMP kinase activity
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0006163biological_processpurine nucleotide metabolic process
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0046037biological_processGMP metabolic process
A0046710biological_processGDP metabolic process
B0000166molecular_functionnucleotide binding
B0004385molecular_functionGMP kinase activity
B0005524molecular_functionATP binding
B0005829cellular_componentcytosol
B0006163biological_processpurine nucleotide metabolic process
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0046037biological_processGMP metabolic process
B0046710biological_processGDP metabolic process
C0000166molecular_functionnucleotide binding
C0004385molecular_functionGMP kinase activity
C0005524molecular_functionATP binding
C0005829cellular_componentcytosol
C0006163biological_processpurine nucleotide metabolic process
C0016301molecular_functionkinase activity
C0016740molecular_functiontransferase activity
C0046037biological_processGMP metabolic process
C0046710biological_processGDP metabolic process
D0000166molecular_functionnucleotide binding
D0004385molecular_functionGMP kinase activity
D0005524molecular_functionATP binding
D0005829cellular_componentcytosol
D0006163biological_processpurine nucleotide metabolic process
D0016301molecular_functionkinase activity
D0016740molecular_functiontransferase activity
D0046037biological_processGMP metabolic process
D0046710biological_processGDP metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues19
Detailsbinding site for residue 5GP A 300
ChainResidue
ASER44
AASP106
AILE107
AGLU108
AGLY111
AARG159
AHOH416
AHOH420
AHOH428
AHOH446
AHOH467
AARG48
AARG51
ATYR60
AGLU79
APHE83
ATYR88
AGLY89
ATHR90

site_idAC2
Number of Residues21
Detailsbinding site for residue ADP A 301
ChainResidue
AGLY21
ATHR22
AGLY23
ALYS24
ASER25
ATHR26
AARG144
AARG148
AASN181
AASP182
ALEU184
AHOH416
AHOH427
AHOH430
AHOH436
AHOH479
AHOH485
AHOH515
AHOH548
AHOH567
AHOH587

site_idAC3
Number of Residues19
Detailsbinding site for residue 5GP B 300
ChainResidue
BSER44
BARG48
BARG51
BTYR60
BGLU79
BPHE83
BTYR88
BGLY89
BTHR90
BASP106
BILE107
BGLU108
BGLY111
BARG159
BHOH402
BHOH419
BHOH448
BHOH469
BHOH483

site_idAC4
Number of Residues21
Detailsbinding site for residue ADP B 301
ChainResidue
BGLY21
BTHR22
BGLY23
BLYS24
BSER25
BTHR26
BARG144
BARG148
BASN181
BASP182
BLEU184
BHOH402
BHOH420
BHOH431
BHOH436
BHOH492
BHOH552
BHOH554
BHOH557
BHOH571
BHOH591

site_idAC5
Number of Residues19
Detailsbinding site for residue 5GP C 300
ChainResidue
CSER44
CARG48
CARG51
CTYR60
CGLU79
CPHE83
CTYR88
CGLY89
CTHR90
CASP106
CILE107
CGLU108
CGLY111
CARG159
CHOH410
CHOH431
CHOH441
CHOH464
CHOH495

site_idAC6
Number of Residues20
Detailsbinding site for residue ADP C 301
ChainResidue
CGLY21
CTHR22
CGLY23
CLYS24
CSER25
CTHR26
CARG144
CARG148
CASN181
CASP182
CLEU184
CHOH422
CHOH441
CHOH443
CHOH450
CHOH462
CHOH475
CHOH507
CHOH518
CHOH565

site_idAC7
Number of Residues19
Detailsbinding site for residue 5GP D 300
ChainResidue
DSER44
DARG48
DARG51
DTYR60
DGLU79
DPHE83
DTYR88
DGLY89
DTHR90
DASP106
DILE107
DGLU108
DGLY111
DARG159
DHOH413
DHOH418
DHOH419
DHOH480
DHOH493

site_idAC8
Number of Residues20
Detailsbinding site for residue ADP D 301
ChainResidue
DGLY21
DTHR22
DGLY23
DLYS24
DSER25
DTHR26
DARG144
DARG148
DASN181
DASP182
DHOH419
DHOH428
DHOH429
DHOH464
DHOH465
DHOH481
DHOH482
DHOH502
DHOH508
DHOH535

Functional Information from PROSITE/UniProt
site_idPS00856
Number of Residues18
DetailsGUANYLATE_KINASE_1 Guanylate kinase-like signature. TTRkpRpgEenGreYhFV
ChainResidueDetails
ATHR46-VAL63

246031

PDB entries from 2025-12-10

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