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2HF8

Crystal structure of HypB from Methanocaldococcus jannaschii in the triphosphate form, in complex with zinc

Functional Information from GO Data
ChainGOidnamespacecontents
A0003924molecular_functionGTPase activity
A0005525molecular_functionGTP binding
A0008270molecular_functionzinc ion binding
A0016151molecular_functionnickel cation binding
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
A0051604biological_processprotein maturation
B0003924molecular_functionGTPase activity
B0005525molecular_functionGTP binding
B0008270molecular_functionzinc ion binding
B0016151molecular_functionnickel cation binding
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
B0051604biological_processprotein maturation
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 301
ChainResidue
ATHR47
AASP75
AGLU120
AGSP300
AHOH468

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 301
ChainResidue
BHOH437
BTHR47
BASP75
BGLU120
BGSP300

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 401
ChainResidue
ACYS95
ACYS127
BCYS95
BZN402

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 402
ChainResidue
AZN401
BCYS95
BHIS96
BCYS127
BHOH462

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 403
ChainResidue
AHIS100
AHIS104
BHIS100
BHIS104

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 404
ChainResidue
AHIS100
AHIS104
BHIS100
BHIS104

site_idAC7
Number of Residues25
DetailsBINDING SITE FOR RESIDUE GSP A 300
ChainResidue
AGLY43
ASER44
AGLY45
ALYS46
ATHR47
ALEU48
AASP75
AARG78
AGLU120
AASN167
ALYS168
AASP170
ASER199
ALEU200
ALYS201
AMG301
AHOH416
AHOH458
AHOH464
AHOH465
AHOH468
BGLU146
BLYS153
BALA174
BVAL175

site_idAC8
Number of Residues26
DetailsBINDING SITE FOR RESIDUE GSP B 300
ChainResidue
AGLU146
ALYS153
AALA174
AVAL175
BILE42
BGLY43
BSER44
BGLY45
BLYS46
BTHR47
BLEU48
BASP75
BARG78
BGLU120
BASN167
BLYS168
BASP170
BLEU171
BSER199
BLEU200
BLYS201
BMG301
BHOH422
BHOH437
BHOH453
BHOH463

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:16807243, ECO:0007744|PDB:2HF8
ChainResidueDetails
ACYS95
AHIS96
ACYS127
BCYS95
BHIS96
BCYS127

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:16807243, ECO:0007744|PDB:2HF8, ECO:0007744|PDB:2HF9
ChainResidueDetails
AHIS100
AHIS104
BHIS100
BHIS104

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PDB entries from 2024-07-17

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