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5AUN

Crystal structure of the HypAB-Ni complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0008270molecular_functionzinc ion binding
A0016151molecular_functionnickel cation binding
A0036211biological_processprotein modification process
A0046872molecular_functionmetal ion binding
A0051604biological_processprotein maturation
B0005524molecular_functionATP binding
B0016226biological_processiron-sulfur cluster assembly
B0016787molecular_functionhydrolase activity
B0016887molecular_functionATP hydrolysis activity
B0046872molecular_functionmetal ion binding
B0051536molecular_functioniron-sulfur cluster binding
B0051539molecular_function4 iron, 4 sulfur cluster binding
B0140663molecular_functionATP-dependent FeS chaperone activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 201
ChainResidue
ACYS73
ACYS76
ACYS110
ACYS113

site_idAC2
Number of Residues4
Detailsbinding site for residue NI A 202
ChainResidue
AMET1
AHIS2
AGLU3
AHIS98

site_idAC3
Number of Residues4
Detailsbinding site for residue URE A 203
ChainResidue
ALEU36
AASP38
ALYS94
AGLU35

site_idAC4
Number of Residues4
Detailsbinding site for residue URE A 204
ChainResidue
AGLU41
APHE64
AHOH356
AHOH387

site_idAC5
Number of Residues5
Detailsbinding site for residue URE A 205
ChainResidue
AILE131
ALYS132
AHOH380
BLYS234
BGLU236

site_idAC6
Number of Residues4
Detailsbinding site for residue CL A 206
ChainResidue
AGLN19
ATHR55
AILE56
AHOH429

site_idAC7
Number of Residues1
Detailsbinding site for residue GOL A 207
ChainResidue
BASP5

site_idAC8
Number of Residues24
Detailsbinding site for residue ADP B 301
ChainResidue
BLYS28
BGLY30
BVAL31
BGLY32
BLYS33
BSER34
BLEU35
BSER160
BLEU162
BASN187
BMET188
BPRO217
BPHE218
BTYR219
BLEU222
BPHE237
BMG302
BHOH411
BHOH412
BHOH421
BHOH423
BHOH489
BHOH519
BHOH538

site_idAC9
Number of Residues6
Detailsbinding site for residue MG B 302
ChainResidue
BSER34
BADP301
BHOH421
BHOH422
BHOH423
BHOH519

site_idAD1
Number of Residues6
Detailsbinding site for residue MG B 303
ChainResidue
AHOH310
AHOH323
BLYS149
BHOH416
BHOH473
BHOH550

site_idAD2
Number of Residues4
Detailsbinding site for residue GOL B 304
ChainResidue
ATRP4
ATYR78
BARG79
BHOH420

Functional Information from PROSITE/UniProt
site_idPS01249
Number of Residues43
DetailsHYPA Hydrogenases expression/synthesis hypA family signature. GelqdVaediVkfAMeqlfagTiaeg.AeIeFveeeavfkCrnC
ChainResidueDetails
AGLY34-CYS76

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:26056269, ECO:0007744|PDB:5AUN, ECO:0007744|PDB:5AUO
ChainResidueDetails
AMET1
AHIS2
AHIS98

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00213, ECO:0000269|PubMed:19769985, ECO:0000269|PubMed:26056269, ECO:0007744|PDB:3A43, ECO:0007744|PDB:3A44, ECO:0007744|PDB:5AUN, ECO:0007744|PDB:5AUO, ECO:0007744|PDB:5AUP
ChainResidueDetails
ACYS73
ACYS76
ACYS110
ACYS113

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PDB entries from 2024-10-30

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